2010_paperD_pt2_ex-rep_en

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Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks

Molecular CellArticleHistone Methylation by PRC2Is Inhibitedby Active Chromatin MarksFrank W.Schmitges,1,6Archana B.Prusty,2,6Mahamadou Faty,1Alexandra Stu¨tzer,3Gondichatnahalli M.Lingaraju,1 Jonathan Aiwazian,1Ragna Sack,1Daniel Hess,1Ling Li,4Shaolian Zhou,4Richard D.Bunker,1Urs Wirth,5Tewis Bouwmeester,5Andreas Bauer,5Nga Ly-Hartig,2Kehao Zhao,4Homan Chan,4Justin Gu,4Heinz Gut,1 Wolfgang Fischle,3Ju¨rg Mu¨ller,2,7,*and Nicolas H.Thoma¨1,*1Friedrich Miescher Institute for Biomedical Research,Maulbeerstrasse66,CH-4058Basel,Switzerland2Genome Biology Unit,EMBL Heidelberg,Meyerhofstrasse1,D-69117Heidelberg,Germany3Laboratory of Chromatin Biochemistry,Max Planck Institute for Biophysical Chemistry,Am Fassberg11,D-37077Go¨ttingen,Germany4China Novartis Institutes for Biomedical Research,Lane898Halei Road,Zhangjiang,Shanghai,China5Novartis Institutes for Biomedical Research,CH-4002Basel,Switzerland6These authors contributed equally to this work7Present address:Max Planck Institute of Biochemistry,Am Klopferspitz18,D-82152Martinsried,Germany*Correspondence:muellerj@biochem.mpg.de(J.M.),nicolas.thoma@fmi.ch(N.H.T.)DOI10.1016/j.molcel.2011.03.025SUMMARYThe Polycomb repressive complex2(PRC2)confers transcriptional repression through histone H3lysine 27trimethylation(H3K27me3).Here,we examined how PRC2is modulated by histone modiﬁcations associated with transcriptionally active chromatin. We provide the molecular basis of histone H3 N terminus recognition by the PRC2Nurf55-Su(z)12 submodule.Binding of H3is lost if lysine4in H3is trimethylated.Weﬁnd that H3K4me3inhibits PRC2 activity in an allosteric fashion assisted by the Su(z)12C terminus.In addition to H3K4me3,PRC2 is inhibited by H3K36me2/3(i.e.,both H3K36me2 and H3K36me3).Direct PRC2inhibition by H3K4me3and H3K36me2/3active marks is con-served in humans,mouse,andﬂy,rendering tran-scriptionally active chromatin refractory to PRC2 H3K27trimethylation.While inhibition is present in plant PRC2,it can be modulated through exchange of the Su(z)12subunit.Inhibition by active chromatin marks,coupled to stimulation by transcriptionally repressive H3K27me3,enables PRC2to autono-mously template repressive H3K27me3without over-writing active chromatin domains.INTRODUCTIONPolycomb(PcG)and trithorax group(trxG)proteins form distinct multiprotein complexes that modify chromatin.These com-plexes are conserved in animals and plants and are required to maintain spatially restricted transcription of HOX and other cell fate determination genes(Henderson and Dean,2004; Pietersen and van Lohuizen,2008;Schuettengruber et al., 2007;Schwartz and Pirrotta,2007).PcG proteins act to repress their target genes while trxG protein complexes are required to keep the same genes active in cells where they must be expressed.Among the PcG protein complexes,Polycomb repressive complex2(PRC2)is a histone methyl-transferase(HMTase) that methylates Lys27of H3(H3K27)(Cao et al.,2002;Czermin et al.,2002;Kuzmichev et al.,2004;Mu¨ller et al.,2002).High levels of H3K27trimethylation(H3K27me3)in the coding region generally correlate with transcription repression(Cao et al., 2008;Nekrasov et al.,2007;Sarma et al.,2008).PRC2contains four core subunits:Enhancer of zeste[E(z),EZH2in mammals], Suppressor of zeste12[Su(z)12,SUZ12in mammals],Extra-sex combs[ESC,EED in mammals]and Nurf55[Rbbp4/ RbAp48and Rbbp7/RbAp46in mammals](reviewed in Schuet-tengruber et al.,2007;Wu et al.,2009).E(z)is the catalytic subunit;it requires Nurf55and Su(z)12for nucleosome associa-tion,whereas ESC is required to boost the catalytic activity of E(z)(Nekrasov et al.,2005).Recent studies reported that ESC binds to H3K27me3and that this interaction stimulates the HMTase activity of the complex(Hansen et al.,2008;Margueron et al.,2009;Xu et al.,2010).The observation that PRC2is able to bind to the same modiﬁcation that it deposits led to a model for propagation of H3K27me3during replication.In this model, recognition of H3K27me3on previously modiﬁed nucleosomes promotes methylation of neighboring nucleosomes that contain newly incorporated unmodiﬁed histone H3(Hansen et al.,2008; Margueron et al.,2009).However,it is unclear how such a positive feedback loop ensures that H3K27trimethylation remains localized to repressed target genes and does not invade the chromatin of nearby active genes.In organisms ranging from yeast to humans,chromatin of actively transcribed genes is marked by H3K4me3, H3K36me2,and H3K36me3modiﬁcations:while H3K4me3is tightly localized at and immediately downstream of the transcrip-tion start site,H3K36me2peaks adjacently in the50coding region and H3K36me3is speciﬁcally enriched in the30coding region(Bell et al.,2008;Santos-Rosa et al.,2002).Among the trxG proteins that keep PcG target genes active are the HMTases Trx and Ash1,which methylate H3K4and H3K36, respectively(Milne et al.,2002;Nakamura et al.,2002;Tanaka330Molecular Cell42,330–341,May6,2011ª2011Elsevier Inc.et al.,2007).Studies in Drosophila showed that Trx and Ash1 play a critical role in antagonizing H3K27trimethylation by PRC2,suggesting a crosstalk between repressive and activating marks(Papp and Mu¨ller,2006;Srinivasan et al.,2008).In this study we investigated how PRC2activity is modulated by chromatin marks typically associated with active transcrip-tion.We found that the Nurf55WD40propeller binds the N terminus of unmodiﬁed histone H3and that H3K4me3 prevents this binding.In the context of the tetrameric PRC2 complex,weﬁnd that H3K4me3and H3K36me2/3(i.e.,both H3-K36me2and H3-K36me3)inhibit histone methylation by PRC2in vitro.Dissection of this process by usingﬂy,human, and plant PRC2complexes suggests that the Su(z)12subunit is important for mediating this inhibition.PRC2thus not only contains the enzymatic activity for H3K27methylation and a recognition site for binding to this modiﬁcation,but it also harbors a control module that triggers inhibition of this activity to prevent deposition of H3K27trimethylation on transcription-ally active genes.PRC2can thus integrate information provided by pre-existing histone modiﬁcations to accurately tune its enzymatic activity within a particular chromatin context.RESULTSStructure of Nurf55Bound to the N Terminusof Histone H3Previous studies reported that Nurf55alone is able to bind to histone H3(Beisel et al.,2002;Hansen et al.,2008;Song et al., 2008;Wysocka et al.,2006)but not to a GST-H3fusion protein (Verreault et al.,1998).By usingﬂuorescence polarization(FP) measurements,we found that Nurf55binds the very N terminus of unmodiﬁed histone H3encompassing residues1–15(H31–15) with a K D of$0.8±0.1m M but does not bind to a histone H319–38 peptide(Figure1A).Crystallographic screening resulted in the successful cocrystallization of Nurf55in complex with an H31–19peptide.After molecular replacement with the known structure of Nurf55(Song et al.,2008),the initial mF oÀDF c differ-ence map showed density for H3residues1–14in bothNurf55molecules in the crystallographic asymmetric unit. Figures1B–1E show the structure of H31–19bound to Drosophila Nurf55,reﬁned to2.7A˚resolution(R/R free=20.1%and25.0%, Table1;Figure S1A,available online).The H3peptide binds to theﬂat surface of the Nurf55WD40propeller(Figure1B),subse-quently referred to as the canonical binding site(c-site)(Gaudet et al.,1996).The H3peptide is held in an acidic pocket(Figures 1C and1E)and traverses the central WD40cavity in a straight line across the propeller(Figure1B).Nurf55binds the H3peptide by contacting H3residues Ala1, Arg2,Lys4,Ala7,and Lys9.Each of these residues forms side-chain speciﬁc contacts with the Nurf55propeller(Figures 1D and1E).The bulk of the molecular recognition is directed toward H3Arg2and Lys4.Ala1sits in a buried pocket with its a-amino group hydrogen bonding to Nurf55Asp252,which recognizes andﬁxes the very N terminus of histone H3.The neighboring Arg2is buried deeper within the WD40propeller fold,with its guanidinium group sandwiched by Nurf55residues Phe325and Tyr185(Figure1D).H3Lys4binds to a well-deﬁned surface pocket on Nurf55located on blade2,near the central cavity of the propeller.Its3-amino group is speciﬁcally coordi-nated by the carboxyl groups of Nurf55residues Glu183andGlu130and through the amide oxygen of Asn132(Figure1E).Lys9is stabilized by hydrophobic interactions on the WD40surface while having its3-amino group held in solvent-exposedfashion(Figure1D).Ser10of histone H3marks the beginningof a turn that inverses the peptide directionality.Histone H3residues Thr11–Lys14become progressively disordered andare no longer speciﬁcally recognized.No interpretable densitywas observed beyond Lys14.Taken together,Nurf55speciﬁcallyrecognizes an extended region of the extreme N terminus ofhistone H3(11residues long,700A˚2buried surface area)in thecanonical ligand binding location of WD40propeller domains. Structure of the Nurf55-Su(z)12Subcomplex of PRC2 The H3-Nurf55structure prompted us to investigate how Nurf55might bind histone tails in the presence of Su(z)12,its interactionpartner in PRC2(Nekrasov et al.,2005;Pasini et al.,2004).Asaﬁrst step we mapped the Nurf55-Su(z)12interaction in detailby carrying out limited proteolysis experiments on reconstitutedDrosophila PRC2,followed by isolation of a Nurf55-Su(z)12subcomplex.Mass spectrometric analysis and pull-down exper-iments with recombinant protein identiﬁed Su(z)12residues73–143[hereafter referred to as Su(z)1273–143]as sufﬁcient forNurf55binding(Figures S1C and S1D).Crystals were obtained when Drosophila Nurf55and Su(z)12residues64–359were set up in the presence of0.01%subtilisinprotease(Dong et al.,2007).After data collection,the structurewas reﬁned to a maximal resolution of2.3A˚(Table1).Molecularreplacement with Nurf55as search model provided clear initialmF oÀDF c difference density for a13amino acid-long Su(z)12 fragment spanning Su(z)12residues79–91(Figures2A–2C).Theﬁnal model was reﬁned to2.3A˚(R/R free=17.5%/20.9%)and veriﬁed by simulated annealing composite-omit maps(Fig-ure S1B).The portion of Su(z)12involved in Nurf55binding willhenceforth be referred to as the Nurf55binding epitope(NBE).The Su(z)12binding site on Nurf55is located on the side of thepropeller between the stem of the N-terminal a helix(a1)andthe PP loop(Figures2A and2B).Binding between Su(z)12andNurf55occurs mostly through hydrophobic interactions in anextended conformation.The interaction surface betweenNurf55and the NBE is large for a peptide,spanning around800A˚2.Sequence alignment between Su(z)12orthologs revealsthat the NBE is highly conserved(53%identity and84%similarity)in animals and in plants(Figure2E).With the exceptionof Su(z)12Arg85,the majority of the conserved Su(z)12NBEresidues engage in hydrophobic packing with Nurf55(Figures2B and2C).Together with the Su(z)12VEFS domain and theC2H2zincﬁnger(C5domain)(Birve et al.,2001),the NBE consti-tutes the only identiﬁable motif in Su(z)12found conserved in allSu(z)12orthologs.The NBE binding site on Nurf55has previously been shown tobe occupied by helix1of histone H4(Figure2D)(Murzina et al.,2008;Song et al.,2008),an epitope not accessible in assemblednucleosomes(Luger et al.,1997).Nurf55binds H4and theSu(z)12NBE epitope in a different mode,and importantly,withopposite directionality(Figure2D).The detailed comparison ofthe Nurf55-Su(z)12structure with that of H4bound to Nurf55Molecular CellAllosteric PRC2Inhibition by H3K4me3/H3K36me3Molecular Cell42,330–341,May6,2011ª2011Elsevier Inc.331strongly suggests that binding of Su(z)12(NBE)and of H4(helix 1)are mutually exclusive (Figure 2D).We therefore refer to the Su(z)12and H4binding site on Nurf55as the S/H -site.Su(z)12fragments that include the NBE have poor solubility by themselves and generally require Nurf55coexpression for solu-bilization.However,we were able to measure binding of a chem-ically synthesized Su(z)1275–93peptide to Nurf55by isothermal titration calorimetry (ITC)and found that the peptide was bound with a K D value of 6.7±0.3m M in a 1:1stoichiometry (Fig-ure 2F).Pull-down experiments with recombinant proteinandFigure 1.Crystal Structure of Nurf55in Complex with a Histone H31–19Peptide(A)Nurf55binds to an H31–15peptide with an afﬁnity of $0.8±0.1m M as measured by FP.It has similar afﬁnity for an H31–31peptide (2.2±0.2m M)but no binding can be detected to an H319–38peptide.(B)Ribbon representation of Nurf55-H31–19.Nurf55is shown in rainbow colors and H31–19is depicted in green.The peptide is bound to the c -site of the WD40propeller.(C)Electrostatic surface potential representation (À10to 10kT/e)of the c -site with the H3peptide shown as a stick model in green.(D)Close-up of the c -site detailing the interactions between Nurf55(yellow)and the H31–19peptide (green),with a water molecule shown as a red sphere.(E)Schematic representation of interactions between the H31–19peptide (green)and Nurf55(yellow).Molecular CellAllosteric PRC2Inhibition by H3K4me3/H3K36me3332Molecular Cell 42,330–341,May 6,2011ª2011Elsevier Inc.streptavidin beads suggest that Su(z)12residues 94–143harbor an additional Nurf55binding site not visible in the structure (Figure S1E).Su(z)12144–359,lacking the N-terminal 143residues,no longer binds to Nurf55.The NBE (residues 79–93)and the region adjacent to the NBE (residues 94–143)are thus required for stable interaction with Nurf55.The extended NBE was found enriched after limited proteolysis and in subsequent gel ﬁltration runs coupled with quantitative mass spectrometry (Figure S1C).As the NBE was the only fragment visible after structure determi-nation,we conclude that it represents the major Su(z)12interac-tion epitope for Nurf55binding.The Nurf55-Su(z)12Complex Binds to Histone H3In order to study the potential interdependence of the identiﬁed Nurf55binding sites we compared binding of Nurf55and Nurf55-Su(z)12to the histone H3N terminus.FP experiments showed similar afﬁnities for binding of a histone H31–15peptide to Nurf55(K D $0.8±0.1m M;Figure 1A)and a Nurf55-Su(z)1273–143complex (K D $0.6±0.1m M;Figure 2G).Importantly,mutation of Nurf55resi-dues contacting H3via its c -site drastically reduced binding to an H31–15peptide (Figure S2A),demonstrating that the Nurf55-Su(z)1273–143complex indeed binds the H31–15peptide through the c -site.We conclude that the presence of Su(z)12is compatible with Nurf55binding to H3via its c -site and that the two binding interactions are not interdependent.The observation that the Su(z)12NBE occupies the same Nurf55pocket that was previously shown to bind to helix 1of histone H4prompted us to test whether the Su(z)1273–143-Nurf55complex could still bind to histone H4.We performed pull-down experiments with a glutathione S-transferase (GST)fusion protein containing histone H41–48(Murzina et al.,2008)and found that H4stably interacted with isolated Nurf55but not with Su(z)1273–143-Nurf55(Figure 2H).In PRC2,the presence of Su(z)12in the Nurf55S/H -site therefore precludes binding to helix 1of histone H4.H3Binding by Nurf55-Su(z)12Is Sensitive to the Methylation Status of Lysine 4We next investigated how posttranslational modiﬁcations of the H3tail affect binding to the Nurf55-Su(z)1273–143complex.Modi-ﬁcations on H3Arg2,Lys9,and Lys14did not change afﬁnity of Nurf55-Su(z)12for the modiﬁed H31–15peptide (Figures S2B and S2D).In contrast,peptides that were mono-,di-,or trimethylated on Lys4were bound with signiﬁcantly reduced afﬁnity exhibiting K D values of 17±3m M (H3K4me1),24±3m M (H3K4me2),and >70m M (H3K4me3),respectively (Figure 2I).The FP binding data were independently conﬁrmed by ITC measurements (Figures S2C–S2F).Together,these ﬁndings are in accord with the structural data,which show that H3K9and H3K14are being held with their 3-amino moiety solvent-exposed,while the H3K4side chain is tightly coordinated (Figure 1E).The additional methyl groups on the H3K43-amino group are expected to progressively decrease afﬁnity because of increased steric clashes within the H3K4binding pocket.H3K27Methylation by PRC2Is Inhibited by Histone H3K4me3MarksWe then examined the effect of H3K4me3modiﬁcations,which are no longer retained by Nurf55-Su(z)12,on the catalytic activity of PRC2.In a ﬁrst set of experiments,we determined PRC2steady-state parameters on histone H31–45peptide substrates that were either unmodiﬁed or methylated at Lys 4.We observed similar K M values for H3and H3K4me3peptides of 0.84±0.21m M and 0.36±0.07m M,respectively (Figure 3A),and similar K M values for SAM (5.42±0.65m M for H3and 10.04±1.56m M for H3K4me3).The turnover rate constant k cat ,however,was 8-fold reduced in the presence of H3K4me3:2.53±0.21min -1for unmodiﬁed H3and 0.32±0.08min -1in the presence of H3K4me3(Figure 3A).While substrate binding is largely unaf-fected,turnover is thus severely inhibited in the presence of H3K4me3.This behavior,which results in a k cat /K M speciﬁcity constant of 7.83103M -1s -1(unmodiﬁed H3)compared to 0.533103M -1s -1(H3K4me3),is consistent with heterotrophic allosteric inhibition of the PRC2HMTase triggered by the pres-ence of the H3K4me3.To investigate the effect of the H3K4me3modiﬁcation on PRC2activity in the context of nucleosomes,we reconstituted mononucleosomes with a trimethyllysine analog (MLA)at Lys4in H3(referred to as H3Kc4me3;Figure S3A)(Simon et al.,2007).We found that total H3K27methylation (measured by incorporation of 14C-labeled methyl groups)was substantially impaired on H3Kc4me3-containing nucleosomes compared to wild-type nucleosomes (Figures S3B and S3C).We used western blot analysis to monitor how levels of H3K27mono-,di-,and trimethylation were affected by the H3Kc4me3modiﬁca-tion.While H3K27me1formation was reduced by more than 50%on H3Kc4me3nucleosomes compared to unmodiﬁed nucleosomes (Figures 3B and 3C),H3K27dimethylationandTable 1.Crystallographic Data and Reﬁnement StatisticsNurf55–Su(z)12Nurf55–H31–19Space Group P212121P212121theses.Molecular CellAllosteric PRC2Inhibition by H3K4me3/H3K36me3Molecular Cell 42,330–341,May 6,2011ª2011Elsevier Inc.333titrant H3:S/H-siteN CNCSu(z)12 79-91Histone H4 31-41PP-loophelix α10.00.51.0 1.52.0 2.5-16.00-14.00-12.00-10.00-8.00-6.00-4.00-2.000.00-2.00-1.50-1.00-0.500.00020406080100120Time (min)µc a l /s e cMolar RatioK C a l /M o l e o f I n j e c t a n tK D = 6.7 ± 0.3 µMtitrant: H31-15DEFGH ICA B protein concentration [µM]Nurf55-Su(z)12protein concentration [µM]00.20.40.60.81.000.20.40.60.81.00.010.11101000.010.1110100Nurf55Nurf55-Su(z)12unmod K4me1K4me2K4me3f r a c t i o n b o u n df r a c t i o n b o u n d G ST -H 41-48 + N u r f 55G S T -H 41-48 + N u r f 55-S u (z )1273-143N u r f 55(m o c k c o n t r o l )N u r f 55-S u (z )1273-143(m o c k c o n t r o l )Nurf55GST-H41-48Su(z)1273-143i np ut i n p u t i n p u t i n p u t G S T -p u l l d o w n G S T -p u l l d o w n G S T -p u l l d o w n G S T -p u l l d o w n Figure 2.Crystal Structure and Characterization of Nurf55in Complex with the Su(z)12Binding Epitope for Nurf55(A)Ribbon representation of Nurf55-Su(z)12.Nurf55(rainbow colors)depicts the WD40domain nomenclature and Su(z)12is shown in magenta.The S/H -site is marked by a dashed box.(B)Detailed interactions of Su(z)12(magenta)with the S/H -site (yellow).Water molecules are depicted as red spheres.(C)Schematic representation of interactions between Su(z)12(magenta)and Nurf55(yellow).(D)Overlay of the backbone trace of Su(z)12(magenta)and the H4helix a 1(orange)(Song et al.,2008)in the S/H -site.(E)Alignment of the Su(z)12NBE with sequences from Drosophila melanogaster (dm,Q9NJG9),mouse (mm,NP_954666),human (hs,AAH15704),Xenopus tropicalis (xt,BC121323),zebraﬁsh (dr,BC078293),and the three Arabidopsis thaliana (at)homologs Fis2(ABB84250),EMF2(NP_199936),and VRN2(NP_567517).Identical residues are highlighted in yellow.(F)ITC proﬁle for binding of a Su(z)1275–93peptide to Nurf55.Data were ﬁtted to a one-site model with stoichiometry of 1:1.The derived K D value is 6.7±0.3m M.(G)Binding of H31–15to Nurf55(0.8±0.1m M)and Nurf55-Su(z)1273–143(0.6±0.1m M)measured by FP.Molecular CellAllosteric PRC2Inhibition by H3K4me3/H3K36me3334Molecular Cell 42,330–341,May 6,2011ª2011Elsevier Inc.trimethylation were impaired by more than 80%by using H3Kc4me3nucleosomes (Figure 3C).In order to ascertain that inhibition of PRC2is indeed due to trimethylation of the aminogroup in the lysine side chain,and not due to the use of the MLA,we performed HMTase assays on H3K4me3-containing nucleosomes generated by native peptide ligation (Shogren-Knaak et al.,2003)and on H3Kc4me0and H3K4A nucleosomes.H3K27mono-,di-,and trimethylation was comparably inhibited on H3K4me3and on H3Kc4me3-containing nucleosomes,but was not affected by H3Kc4me0and H3K4A (Figures S3D and S3E).We conclude that H3K4me3speciﬁcally inhibits PRC2-mediated H3K27methylation with the most pronounced inhibi-tory effects observed for H3K27di-and trimethylation.We next tested whether the H3K4me3modiﬁcation affects PRC2nucleosome binding.In electrophoretic mobility shift assays (EMSA),we found that PRC2binds unmodiﬁed or H3Kc4me3-modiﬁed nucleosomes with comparable afﬁnity (Fig-ure S4A).Even though binding of Nurf55to the N terminus of ABC571141712290286571141712290286unmodified H3Kc4me3H3K27me3H4dmPRC2 [nM]H3K27me2H4H3K27me1H4H3K27me1H3K27me3H3K27me2dmPRC2 + unmod H3dmPRC2 + H3Kc4me3r e l a t i v e H M T a s e a c t i v i t ySubstrate Apparent Km of SAM (µM)Apparent Km of peptide (nM)k cat (min )-1k cat /Km (M S )-1-1H31-45 -biotin H3K4me31-45 -biotin5.42 ± 0.6510.04 ± 1.56355 ± 74.60.32 ± 0.080.53 x 10836 ± 207 2.53 ± 0.217.8 x 1033Figure 3.HMTase Activity of PRC2Is In-hibited by H3K4me3Marks(A)HMTase assay with PRC2and H31–45-biotin peptides measuring the concentration of SAH produced by the enzymatic reaction.When an H3K4me3-modiﬁed peptide is used,the speciﬁcity constant (k cat /K M )is drastically reduced,indicative of heterotrophic allosteric inhibition.(B)Western blot-based HMTase assay by using recombinant Drosophila mononucleosomes (571nM)and increasing amounts of PRC2.HMTase activity was monitored with antibodies against H3K27me1,H3K27me2,or H3K27me3as indicated;in each case the membrane was also probed with an antibody against unmodiﬁed histone H4to control for equal loading and western blot processing.Deposition of K27di-and trime-thylation is drastically reduced when nucleosomes are used that carry a H3Kc4me3modiﬁcation.(C)Quantiﬁcation of HMTase activity of Drosophila PRC2(286nM)on unmodiﬁed and H3Kc4me3-modiﬁed nucleosomes by quantitative western blotting.histone H3is almost 100-fold reduced byH3K4me3(Figure 2I and Figure S2F),inter-action of the Nurf55c -site with H3K4does not seem to make a detectable con-tribution to nucleosome binding by PRC2in this assay.Consistent with the allosteric mechanism of H3K4me3inhibition that we had observed in the peptide assays (Figure 3A),inhibition of the PRC2HMTase activity by H3K4me3-containingnucleosomes is not caused by impaired nucleosome binding,but is rather the consequence of reduced catalytic turnover.H3K4me3Needs to Be Present on the Same Tail as K27to Inhibit PRC2We then assessed whether inhibition of the PRC2HMTase activity by H3K4me3requires the K4me3mark to be located on the substrate nucleosome (in cis ),or whether it could also be trig-gered if the H3K4me3modiﬁcation was provided on a separate peptide (in trans ).We performed HMTase assays on unmodiﬁed oligonucleosomes in the presence of increasing amounts of a histone H31–15peptide trimethylated at K4(H31–15-K4me3)(Figure 4A).Addition of the H31–15-K4me3peptide did not affect PRC2HMTase activity at peptide concentrations as high as $200m M.When testing H31–19-unmodiﬁed peptide in controls at comparable concentrations,we did observe concentration-dependent PRC2inhibition (Figure 4A),probably because of substrate competition at large peptide excess.As H3K4me3-(H)GST pull-down assay with recombinant GST-H41–48and Nurf55and Nurf55-Su(z)1273–143proteins.GST-H41–48is able to bind Nurf55alone but in the Nurf55-Su(z)1273–143complex the binding site is occupied by Su(z)12(left panel).Control pull-downs with GST beads and either Nurf55or Nurf55-Su(z)1273–143alone showed no unspeciﬁc binding (right panel).(I)Binding of different H31–15peptides to Nurf55-Su(z)1273–143measured by FP.While unmodiﬁed H3is bound with 0.8±0.1m M afﬁnity,methylation of Lys 4drastically reduces binding afﬁnity (17±3m M for K4me1,24±3m M for K4me2,and >70m M for K4me3).Molecular CellAllosteric PRC2Inhibition by H3K4me3/H3K36me3Molecular Cell 42,330–341,May 6,2011ª2011Elsevier Inc.335modiﬁed peptides did not show this competitive behavior,we conclude that PRC2is not inhibited by H3K4me3in trans and that H3K4me3and unmodiﬁed H3peptides are probably bound to PRC2in a different fashion.Analogously,we saw no inhibition when testing the effect of H3K4me3in trans by using peptides as substrates (Figure S4B ).Taken together,our ﬁndings strongly argue that H3K4me3only inhibits PRC2if present on the same tail that contains the H3K27target lysine (in cis ).Previous studies reported that addition of H3K27me3peptides in trans enhances H3K27methylation of oligonucleosomes by human PRC2through binding to the EED WD40domain (Margueron et al.,2009;Xu et al.,2010).We tested whether addition of H3K27me3peptides in trans would stimulate H3K27methylation by PRC2on H3Kc4me3-modiﬁed nucleosomes.We observed that the inhibitory effect of H3Kc4me3-containing nucleosomes can,at least in part,be overcome through addition of high concentrations of H3K27me3peptides (Figure 4B and Figure S4C).PRC2is therefore able to simultaneously integrate inhibitory (H3K4me3)and activating (H3K27me3)chromatin signatures and adjust its enzymatic activity in response to the surrounding epigenetic environment.PRC2Inhibition of H3K4me3Is Conserved in Mammalian PRC2Our results with Drosophila PRC2prompted us to investigate to what extent inhibition by H3K4me3is an evolutionarily conserved mechanism.H3K27methylation by human and mouse PRC2on nucleosome substrates carrying H3Kc4me3modiﬁcations was also strongly inhibited,comparable to the inhibition observed for Drosophila PRC2(Figure 5A and Figure S5A).The Su(z)12Subunit Codetermines Whether PRC2Is Inhibited by H3K4me3In Arabidopsis thaliana ,three different E(z)homologs combined with three Su(z)12homologs have been described.The distinct PRC2complexes in plants harboring the different E(z)or Su(z)12subunits are implicated in the control of distinct developmental processes during Arabidopsis development (He,2009).In this study we focused on PRC2complexes con-taining the E(z)homolog CURLY LEAF (CLF).We expressed and reconstituted the Arabidopsis PRC2complex comprising CLF,FERTILIZATION INDEPENDENT ENDOSPERM (FIE,a homolog of ESC),EMBRYONIC FLOWER 2(EMF2,a homolog of Su(z)12),and MULTICOPY SUPPRESSOR OF IRA (MSI1,a homolog of Nurf55).We found that CLF indeed functions as a H3K27me3HMTase (Figure 5B).Moreover,H3K27methylation by the CLF-FIE-EMF2-MSI1complex on nucleosome arrays containing H3Kc4me3was inhibited (Figure 5B)in a manner comparable to human or Drosophila PRC2.We next tested a related Arabidopsis PRC2complex again composed of CLF,FIE,and MSI1but containing the Su(z)12homolog vernalization 2(VRN2)instead of EMF2.The VRN2protein is speciﬁcally implicated as a repressor of the FLC locus,thereby controlling ﬂowering time in response to vernalization (reviewed in Henderson and Dean,2004).The CLF-FIE-MSI1-VRN2complex was active on unmodiﬁed nucleosomes but,strikingly,it was not inhibited on H3Kc4me3-modiﬁed nucle-osomes (Figure 5C).Substitution of a single subunit (i.e.,EMF2by VRN2)thus renders the complex nonresponsive to the H3K4methylation state.While PRC2inhibition by H3K4me3appears hardwired in mammals and ﬂies,in which only a single-Su(z)12ortholog is present,Arabidopsis inhibition can be enabled or disabled through exchange of the Su(z)12homolog.The Su(z)12C Terminus Harboring the VEFS Domain Is the Minimal Su(z)12Domain Required for Activation and Active Mark InhibitionThe importance of the Su(z)12subunit in active mark H3K4me3inhibition prompted us to map the Su(z)12domains required for inhibition.Previous ﬁndings showed that E(z)or E(z)-ESC in the absence of Su(z)12is enzymatically inactive (Nekrasov et al.,2005).Moreover,the VEFS domain (Birve et al.,2001)was found to be the major E(z)binding domain (Ketel et al.,2005).We reconstituted mouse PRC2complexes containing EZH2,EED,and either SUZ12C 2H 2domain +VEFS (residues 439–741)or SUZ12VEFS alone (residues 552–741).Both of these minimal complexes were active in HMTase assays on nucleosomes (Figure 5D)but with lower activity than that of the full PRC2complex.We therefore focused on formation ofAB26511030206H3K27me3H4peptides in trans[µM]H3K27me2H4H3K27me1H4H3 unmod H3K4me3H3K36me326511032062651103206n o e n z ym e26511030H3K27me3H4peptides in trans[µM]H3K27me2H4H3K27me1H4H3K27me3n oe n z y m eFigure 4.PRC2Activity Is Not Inhibited by H3K4me3Peptides in trans(A)Western blot-based HMTase assay by using unmodiﬁed 4-mer oligonu-cleosomes (36nM)and increasing amounts of H3peptides added in trans .Enzyme concentration was kept constant at 86nM.Western blots were pro-cessed as described in Figure 3B.HMTase activity is inhibited by an unmodiﬁed H31–19peptide (left),but not by H3K4me3-or H3K36me3-modiﬁed peptides.(B)HMTase assay with H3Kc4me3-modiﬁed oligonucleosomes (36nM),86nM PRC2,and H3K27me3peptide in trans .Western blots were processed as described in Figure 3B.HMTase activity of PRC2can be stimulated by the H3K27me3peptide even on inhibiting substrate leading to increased levels of H3K27di-and trimethylation.Molecular CellAllosteric PRC2Inhibition by H3K4me3/H3K36me3336Molecular Cell 42,330–341,May 6,2011ª2011Elsevier Inc.。

IEEE Std 1159-1995,IEEE Recommended Practice for Monitoring Electric Power Quality

IEEE Std 1159-1995 IEEE Recommended Practice for Monitoring Electric Power QualitySponsorIEEE Standards Coordinating Committee 22 onPower QualityApproved June 14, 1995IEEE Standards BoardAbstract: The monitoring of electric power quality of ac power systems, definitions of power quality terminology, impact of poor power quality on utility and customer equipment, and the measurement of electromagnetic phenomena are covered.Keywords: data interpretation, electric power quality, electromagnetic phenomena, monitoring, power quality definitionsIEEE Standards documents are developed within the Technical Committees of the IEEE Societies and the Standards Coordinating Committees of the IEEE Standards Board. Members of the committees serve voluntarily and without compensation. They are not necessarily members of the Institute. The standards developed within IEEE represent a consensus of the broad expertise on the subject within the Institute as well as those activities outside of IEEE that have expressed an interest in partici-pating in the development of the standard.Use of an IEEE Standard is wholly voluntary. The existence of an IEEE Standard does not imply that there are no other ways to produce, test, measure, purchase, mar-ket, or provide other goods and services related to the scope of the IEEE Standard. Furthermore, the viewpoint expressed at the time a standard is approved and issued is subject to change brought about through developments in the state of the art and com-ments received from users of the standard. Every IEEE Standard is subjected to review at least every Þve years for revision or reafÞrmation. When a document is more than Þve years old and has not been reafÞrmed, it is reasonable to conclude that its contents, although still of some value, do not wholly reßect the present state of the art. Users are cautioned to check to determine that they have the latest edition of any IEEE Standard.Comments for revision of IEEE Standards are welcome from any interested party, regardless of membership afÞliation with IEEE. Suggestions for changes in docu-ments should be in the form of a proposed change of text, together with appropriate supporting comments.Interpretations: Occasionally questions may arise regarding the meaning of portions of standards as they relate to speciÞc applications. When the need for interpretations is brought to the attention of IEEE, the Institute will initiate action to prepare appro-priate responses. Since IEEE Standards represent a consensus of all concerned inter-ests, it is important to ensure that any interpretation has also received the concurrence of a balance of interests. For this reason IEEE and the members of its technical com-mittees are not able to provide an instant response to interpretation requests except in those cases where the matter has previously received formal consideration.Comments on standards and requests for interpretations should be addressed to:Secretary, IEEE Standards Board445 Hoes LaneP.O. Box 1331Piscataway, NJ 08855-1331USAIntroduction(This introduction is not part of IEEE Std 1159-1995, IEEE Recommended Practice for Monitoring Electric Power Quality.)This recommended practice was developed out of an increasing awareness of the difÞculty in comparing results obtained by researchers using different instruments when seeking to characterize the quality of low-voltage power systems. One of the initial goals was to promote more uniformity in the basic algorithms and data reduction methods applied by different instrument manufacturers. This proved difÞcult and was not achieved, given the free market principles under which manufacturers design and market their products. However, consensus was achieved on the contents of this recommended practice, which provides guidance to users of monitoring instruments so that some degree of comparisons might be possible.An important Þrst step was to compile a list of power quality related deÞnitions to ensure that contributing parties would at least speak the same language, and to provide instrument manufacturers with a common base for identifying power quality phenomena. From that starting point, a review of the objectives of moni-toring provides the necessary perspective, leading to a better understanding of the means of monitoringÑthe instruments. The operating principles and the application techniques of the monitoring instruments are described, together with the concerns about interpretation of the monitoring results. Supporting information is provided in a bibliography, and informative annexes address calibration issues.The Working Group on Monitoring Electric Power Quality, which undertook the development of this recom-mended practice, had the following membership:J. Charles Smith, Chair Gil Hensley, SecretaryLarry Ray, Technical EditorMark Andresen Thomas Key John RobertsVladi Basch Jack King Anthony St. JohnRoger Bergeron David Kreiss Marek SamotyjJohn Burnett Fran•ois Martzloff Ron SmithJohn Dalton Alex McEachern Bill StuntzAndrew Dettloff Bill Moncrief John SullivanDave GrifÞth Allen Morinec David VannoyThomas Gruzs Ram Mukherji Marek WaclawlakErich Gunther Richard Nailen Daniel WardMark Kempker David Pileggi Steve WhisenantHarry RauworthIn addition to the working group members, the following people contributed their knowledge and experience to this document:Ed Cantwell Christy Herig Tejindar SinghJohn Curlett Allan Ludbrook Maurice TetreaultHarshad MehtaiiiThe following persons were on the balloting committee:James J. Burke David Kreiss Jacob A. RoizDavid A. Dini Michael Z. Lowenstein Marek SamotyjW. Mack Grady Fran•ois D. Martzloff Ralph M. ShowersDavid P. Hartmann Stephen McCluer J. C. SmithMichael Higgins A. McEachern Robert L. SmithThomas S. Key W. A. Moncrief Daniel J. WardJoseph L. KoepÞnger P. Richman Charles H. WilliamsJohn M. RobertsWhen the IEEE Standards Board approved this standard on June 14, 1995, it had the following membership:E. G. ÒAlÓ Kiener, Chair Donald C. Loughry,Vice ChairAndrew G. Salem,SecretaryGilles A. Baril Richard J. Holleman Marco W. MigliaroClyde R. Camp Jim Isaak Mary Lou PadgettJoseph A. Cannatelli Ben C. Johnson John W. PopeStephen L. Diamond Sonny Kasturi Arthur K. ReillyHarold E. Epstein Lorraine C. Kevra Gary S. RobinsonDonald C. Fleckenstein Ivor N. Knight Ingo RuschJay Forster*Joseph L. KoepÞnger*Chee Kiow TanDonald N. Heirman D. N. ÒJimÓ Logothetis Leonard L. TrippL. Bruce McClung*Member EmeritusAlso included are the following nonvoting IEEE Standards Board liaisons:Satish K. AggarwalRichard B. EngelmanRobert E. HebnerChester C. TaylorRochelle L. SternIEEE Standards Project EditorivContentsCLAUSE PAGE 1.Overview (1)1.1Scope (1)1.2Purpose (2)2.References (2)3.Definitions (2)3.1Terms used in this recommended practice (2)3.2Avoided terms (7)3.3Abbreviations and acronyms (8)4.Power quality phenomena (9)4.1Introduction (9)4.2Electromagnetic compatibility (9)4.3General classification of phenomena (9)4.4Detailed descriptions of phenomena (11)5.Monitoring objectives (24)5.1Introduction (24)5.2Need for monitoring power quality (25)5.3Equipment tolerances and effects of disturbances on equipment (25)5.4Equipment types (25)5.5Effect on equipment by phenomena type (26)6.Measurement instruments (29)6.1Introduction (29)6.2AC voltage measurements (29)6.3AC current measurements (30)6.4Voltage and current considerations (30)6.5Monitoring instruments (31)6.6Instrument power (34)7.Application techniques (35)7.1Safety (35)7.2Monitoring location (38)7.3Equipment connection (41)7.4Monitoring thresholds (43)7.5Monitoring period (46)8.Interpreting power monitoring results (47)8.1Introduction (47)8.2Interpreting data summaries (48)8.3Critical data extraction (49)8.4Interpreting critical events (51)8.5Verifying data interpretation (59)vANNEXES PAGE Annex A Calibration and self testing (informative) (60)A.1Introduction (60)A.2Calibration issues (61)Annex B Bibliography (informative) (63)B.1Definitions and general (63)B.2Susceptibility and symptomsÑvoltage disturbances and harmonics (65)B.3Solutions (65)B.4Existing power quality standards (67)viIEEE Recommended Practice for Monitoring Electric Power Quality1. Overview1.1 ScopeThis recommended practice encompasses the monitoring of electric power quality of single-phase and polyphase ac power systems. As such, it includes consistent descriptions of electromagnetic phenomena occurring on power systems. The document also presents deÞnitions of nominal conditions and of deviations from these nominal conditions, which may originate within the source of supply or load equipment, or from interactions between the source and the load.Brief, generic descriptions of load susceptibility to deviations from nominal conditions are presented to identify which deviations may be of interest. Also, this document presents recommendations for measure-ment techniques, application techniques, and interpretation of monitoring results so that comparable results from monitoring surveys performed with different instruments can be correlated.While there is no implied limitation on the voltage rating of the power system being monitored, signal inputs to the instruments are limited to 1000 Vac rms or less. The frequency ratings of the ac power systems being monitored are in the range of 45Ð450 Hz.Although it is recognized that the instruments may also be used for monitoring dc supply systems or data transmission systems, details of application to these special cases are under consideration and are not included in the scope. It is also recognized that the instruments may perform monitoring functions for envi-ronmental conditions (temperature, humidity, high frequency electromagnetic radiation); however, the scope of this document is limited to conducted electrical parameters derived from voltage or current measure-ments, or both.Finally, the deÞnitions are solely intended to characterize common electromagnetic phenomena to facilitate communication between various sectors of the power quality community. The deÞnitions of electromagnetic phenomena summarized in table 2 are not intended to represent performance standards or equipment toler-ances. Suppliers of electricity may utilize different thresholds for voltage supply, for example, than the ±10% that deÞnes conditions of overvoltage or undervoltage in table 2. Further, sensitive equipment may mal-function due to electromagnetic phenomena not outside the thresholds of the table 2 criteria.1IEEEStd 1159-1995IEEE RECOMMENDED PRACTICE FOR 1.2 PurposeThe purpose of this recommended practice is to direct users in the proper monitoring and data interpretation of electromagnetic phenomena that cause power quality problems. It deÞnes power quality phenomena in order to facilitate communication within the power quality community. This document also forms the con-sensus opinion about safe and acceptable methods for monitoring electric power systems and interpreting the results. It further offers a tutorial on power system disturbances and their common causes.2. ReferencesThis recommended practice shall be used in conjunction with the following publications. When the follow-ing standards are superseded by an approved revision, the revision shall apply.IEC 1000-2-1 (1990), Electromagnetic Compatibility (EMC)ÑPart 2 Environment. Section 1: Description of the environmentÑelectromagnetic environment for low-frequency conducted disturbances and signaling in public power supply systems.1IEC 50(161)(1990), International Electrotechnical V ocabularyÑChapter 161: Electromagnetic Compatibility. IEEE Std 100-1992, IEEE Standard Dictionary of Electrical and Electronic Terms (ANSI).2IEEE Std 1100-1992, IEEE Recommended Practice for Powering and Grounding Sensitive Electronic Equipment (Emerald Book) (ANSI).3. DeÞnitionsThe purpose of this clause is to present concise deÞnitions of words that convey the basic concepts of power quality monitoring. These terms are listed below and are expanded in clause 4. The power quality commu-nity is also pervaded by terms that have no scientiÞc deÞnition. A partial listing of these words is included in 3.2; use of these terms in the power quality community is discouraged. Abbreviations and acronyms that are employed throughout this recommended practice are listed in 3.3.3.1 Terms used in this recommended practiceThe primary sources for terms used are IEEE Std 100-19923 indicated by (a), and IEC 50 (161)(1990) indi-cated by (b). Secondary sources are IEEE Std 1100-1992 indicated by (c), IEC-1000-2-1 (1990) indicated by (d) and UIE -DWG-3-92-G [B16]4. Some referenced deÞnitions have been adapted and modiÞed in order to apply to the context of this recommended practice.3.1.1 accuracy: The freedom from error of a measurement. Generally expressed (perhaps erroneously) as percent inaccuracy. Instrument accuracy is expressed in terms of its uncertaintyÑthe degree of deviation from a known value. An instrument with an uncertainty of 0.1% is 99.9% accurate. At higher accuracy lev-els, uncertainty is typically expressed in parts per million (ppm) rather than as a percentage.1IEC publications are available from IEC Sales Department, Case Postale 131, 3, rue de VarembŽ, CH-1211, Gen•ve 20, Switzerland/ Suisse. IEC publications are also available in the United States from the Sales Department, American National Standards Institute, 11 West 42nd Street, 13th Floor, New York, NY 10036, USA.2IEEE publications are available from the Institute of Electrical and Electronics Engineers, 445 Hoes Lane, P.O. Box 1331, Piscataway, NJ 08855-1331, USA.3Information on references can be found in clause 2.4The numbers in brackets correspond to those bibliographical items listed in annex B.2IEEE MONITORING ELECTRIC POWER QUALITY Std 1159-1995 3.1.2 accuracy ratio: The ratio of an instrumentÕs tolerable error to the uncertainty of the standard used to calibrate it.3.1.3 calibration: Any process used to verify the integrity of a measurement. The process involves compar-ing a measuring instrument to a well defined standard of greater accuracy (a calibrator) to detect any varia-tions from specified performance parameters, and making any needed compensations. The results are then recorded and filed to establish the integrity of the calibrated instrument.3.1.4 common mode voltage: A voltage that appears between current-carrying conductors and ground.b The noise voltage that appears equally and in phase from each current-carrying conductor to ground.c3.1.5 commercial power: Electrical power furnished by the electric power utility company.c3.1.6 coupling: Circuit element or elements, or network, that may be considered common to the input mesh and the output mesh and through which energy may be transferred from one to the other.a3.1.7 current transformer (CT): An instrument transformer intended to have its primary winding con-nected in series with the conductor carrying the current to be measured or controlled.a3.1.8 dip: See: sag.3.1.9 dropout: A loss of equipment operation (discrete data signals) due to noise, sag, or interruption.c3.1.10 dropout voltage: The voltage at which a device fails to operate.c3.1.11 electromagnetic compatibility: The ability of a device, equipment, or system to function satisfacto-rily in its electromagnetic environment without introducing intolerable electromagnetic disturbances to any-thing in that environment.b3.1.12 electromagnetic disturbance: Any electromagnetic phenomena that may degrade the performance of a device, equipment, or system, or adversely affect living or inert matter.b3.1.13 electromagnetic environment: The totality of electromagnetic phenomena existing at a given location.b3.1.14 electromagnetic susceptibility: The inability of a device, equipment, or system to perform without degradation in the presence of an electromagnetic disturbance.NOTEÑSusceptibility is a lack of immunity.b3.1.15 equipment grounding conductor: The conductor used to connect the noncurrent-carrying parts of conduits, raceways, and equipment enclosures to the grounded conductor (neutral) and the grounding elec-trode at the service equipment (main panel) or secondary of a separately derived system (e.g., isolation transformer). See Section 100 in ANSI/NFPA 70-1993 [B2].3.1.16 failure mode: The effect by which failure is observed.a3.1.17 ßicker: Impression of unsteadiness of visual sensation induced by a light stimulus whose luminance or spectral distribution fluctuates with time.b3.1.18 frequency deviation: An increase or decrease in the power frequency. The duration of a frequency deviation can be from several cycles to several hours.c Syn.: power frequency variation.3.1.19 fundamental (component): The component of an order 1 (50 or 60 Hz) of the Fourier series of a periodic quantity.b3IEEEStd 1159-1995IEEE RECOMMENDED PRACTICE FOR 3.1.20 ground: A conducting connection, whether intentional or accidental, by which an electric circuit or piece of equipment is connected to the earth, or to some conducting body of relatively large extent that serves in place of the earth.NOTEÑ It is used for establishing and maintaining the potential of the earth (or of the conducting body) or approxi-mately that potential, on conductors connected to it, and for conducting ground currents to and from earth (or the con-ducting body).a3.1.21 ground loop: In a radial grounding system, an undesired conducting path between two conductive bodies that are already connected to a common (single-point) ground.3.1.22 harmonic (component): A component of order greater than one of the Fourier series of a periodic quantity.b3.1.23 harmonic content: The quantity obtained by subtracting the fundamental component from an alter-nating quantity.a3.1.24 immunity (to a disturbance): The ability of a device, equipment, or system to perform without deg-radation in the presence of an electromagnetic disturbance.b3.1.25 impulse: A pulse that, for a given application, approximates a unit pulse.b When used in relation to the monitoring of power quality, it is preferred to use the term impulsive transient in place of impulse.3.1.26 impulsive transient: A sudden nonpower frequency change in the steady-state condition of voltage or current that is unidirectional in polarity (primarily either positive or negative).3.1.27 instantaneous: A time range from 0.5Ð30 cycles of the power frequency when used to quantify the duration of a short duration variation as a modifier.3.1.28 interharmonic (component): A frequency component of a periodic quantity that is not an integer multiple of the frequency at which the supply system is designed to operate operating (e.g., 50 Hz or 60 Hz).3.1.29 interruption, momentary (power quality monitoring): A type of short duration variation. The complete loss of voltage (< 0.1 pu) on one or more phase conductors for a time period between 0.5 cycles and 3 s.3.1.30 interruption, sustained (electric power systems): Any interruption not classified as a momentary interruption.3.1.31 interruption, temporary (power quality monitoring):A type of short duration variation. The com-plete loss of voltage (< 0.1 pu) on one or more phase conductors for a time period between 3 s and 1 min.3.1.32 isolated ground: An insulated equipment grounding conductor run in the same conduit or raceway as the supply conductors. This conductor may be insulated from the metallic raceway and all ground points throughout its length. It originates at an isolated ground-type receptacle or equipment input terminal block and terminates at the point where neutral and ground are bonded at the power source. See Section 250-74, Exception #4 and Exception in Section 250-75 in ANSI/NFPA 70-1993 [B2].3.1.33 isolation: Separation of one section of a system from undesired influences of other sections.c3.1.34 long duration voltage variation:See: voltage variation, long duration.3.1.35 momentary (power quality monitoring): A time range at the power frequency from 30 cycles to 3 s when used to quantify the duration of a short duration variation as a modifier.4IEEE MONITORING ELECTRIC POWER QUALITY Std 1159-1995 3.1.36 momentary interruption:See: interruption, momentary.3.1.37 noise: Unwanted electrical signals which produce undesirable effects in the circuits of the control systems in which they occur.a (For this document, control systems is intended to include sensitive electronic equipment in total or in part.)3.1.38 nominal voltage (Vn): A nominal value assigned to a circuit or system for the purpose of conve-niently designating its voltage class (as 120/208208/120, 480/277, 600).d3.1.39 nonlinear load: Steady-state electrical load that draws current discontinuously or whose impedance varies throughout the cycle of the input ac voltage waveform.c3.1.40 normal mode voltage: A voltage that appears between or among active circuit conductors, but not between the grounding conductor and the active circuit conductors.3.1.41 notch: A switching (or other) disturbance of the normal power voltage waveform, lasting less than 0.5 cycles, which is initially of opposite polarity than the waveform and is thus subtracted from the normal waveform in terms of the peak value of the disturbance voltage. This includes complete loss of voltage for up to 0.5 cycles [B13].3.1.42 oscillatory transient: A sudden, nonpower frequency change in the steady-state condition of voltage or current that includes both positive or negative polarity value.3.1.43 overvoltage: When used to describe a specific type of long duration variation, refers to a measured voltage having a value greater than the nominal voltage for a period of time greater than 1 min. Typical val-ues are 1.1Ð1.2 pu.3.1.44 phase shift: The displacement in time of one waveform relative to another of the same frequency and harmonic content.c3.1.45 potential transformer (PT): An instrument transformer intended to have its primary winding con-nected in shunt with a power-supply circuit, the voltage of which is to be measured or controlled. Syn.: volt-age transformer.a3.1.46 power disturbance: Any deviation from the nominal value (or from some selected thresholds based on load tolerance) of the input ac power characteristics.c3.1.47 power quality: The concept of powering and grounding sensitive equipment in a manner that is suit-able to the operation of that equipment.cNOTEÑWithin the industry, alternate definitions or interpretations of power quality have been used, reflecting different points of view. Therefore, this definition might not be exclusive, pending development of a broader consensus.3.1.48 precision: Freedom from random error.3.1.49 pulse: An abrupt variation of short duration of a physical an electrical quantity followed by a rapid return to the initial value.3.1.50 random error: Error that is not repeatable, i.e., noise or sensitivity to changing environmental factors. NOTEÑFor most measurements, the random error is small compared to the instrument tolerance.3.1.51 sag: A decrease to between 0.1 and 0.9 pu in rms voltage or current at the power frequency for dura-tions of 0.5 cycle to 1 min. Typical values are 0.1 to 0.9 pu.b See: dip.IEEEStd 1159-1995IEEE RECOMMENDED PRACTICE FOR NOTEÑTo give a numerical value to a sag, the recommended usage is Òa sag to 20%,Ó which means that the line volt-age is reduced down to 20% of the normal value, not reduced by 20%. Using the preposition ÒofÓ (as in Òa sag of 20%,Óor implied by Òa 20% sagÓ) is deprecated.3.1.52 shield: A conductive sheath (usually metallic) normally applied to instrumentation cables, over the insulation of a conductor or conductors, for the purpose of providing means to reduce coupling between the conductors so shielded and other conductors that may be susceptible to, or that may be generating unwanted electrostatic or electromagnetic fields (noise).c3.1.53 shielding: The use of a conducting and/or ferromagnetic barrier between a potentially disturbing noise source and sensitive circuitry. Shields are used to protect cables (data and power) and electronic cir-cuits. They may be in the form of metal barriers, enclosures, or wrappings around source circuits and receiv-ing circuits.c3.1.54 short duration voltage variation:See: voltage variation, short duration.3.1.55 slew rate: Rate of change of ac voltage, expressed in volts per second a quantity such as volts, fre-quency, or temperature.a3.1.56 sustained: When used to quantify the duration of a voltage interruption, refers to the time frame asso-ciated with a long duration variation (i.e., greater than 1 min).3.1.57 swell: An increase in rms voltage or current at the power frequency for durations from 0.5 cycles to 1 min. Typical values are 1.1Ð1.8 pu.3.1.58 systematic error: The portion of error that is repeatable, i.e., zero error, gain or scale error, and lin-earity error.3.1.59 temporary interruption:See: interruption, temporary.3.1.60 tolerance: The allowable variation from a nominal value.3.1.61 total harmonic distortion disturbance level: The level of a given electromagnetic disturbance caused by the superposition of the emission of all pieces of equipment in a given system.b The ratio of the rms of the harmonic content to the rms value of the fundamental quantity, expressed as a percent of the fun-damental [B13].a Syn.: distortion factor.3.1.62 traceability: Ability to compare a calibration device to a standard of even higher accuracy. That stan-dard is compared to another, until eventually a comparison is made to a national standards laboratory. This process is referred to as a chain of traceability.3.1.63 transient: Pertaining to or designating a phenomenon or a quantity that varies between two consecu-tive steady states during a time interval that is short compared to the time scale of interest. A transient can be a unidirectional impulse of either polarity or a damped oscillatory wave with the first peak occurring in either polarity.b3.1.64 undervoltage: A measured voltage having a value less than the nominal voltage for a period of time greater than 1 min when used to describe a specific type of long duration variation, refers to. Typical values are 0.8Ð0.9 pu.3.1.65 voltage change: A variation of the rms or peak value of a voltage between two consecutive levels sustained for definite but unspecified durations.d3.1.66 voltage dip:See: sag.IEEE MONITORING ELECTRIC POWER QUALITY Std 1159-1995 3.1.67 voltage distortion: Any deviation from the nominal sine wave form of the ac line voltage.3.1.68 voltage ßuctuation: A series of voltage changes or a cyclical variation of the voltage envelope.d3.1.69 voltage imbalance (unbalance), polyphase systems: The maximum deviation among the three phases from the average three-phase voltage divided by the average three-phase voltage. The ratio of the neg-ative or zero sequence component to the positive sequence component, usually expressed as a percentage.a3.1.70 voltage interruption: Disappearance of the supply voltage on one or more phases. Usually qualified by an additional term indicating the duration of the interruption (e.g., momentary, temporary, or sustained).3.1.71 voltage regulation: The degree of control or stability of the rms voltage at the load. Often specified in relation to other parameters, such as input-voltage changes, load changes, or temperature changes.c3.1.72 voltage variation, long duration: A variation of the rms value of the voltage from nominal voltage for a time greater than 1 min. Usually further described using a modifier indicating the magnitude of a volt-age variation (e.g., undervoltage, overvoltage, or voltage interruption).3.1.73 voltage variation, short duration: A variation of the rms value of the voltage from nominal voltage for a time greater than 0.5 cycles of the power frequency but less than or equal to 1 minute. Usually further described using a modifier indicating the magnitude of a voltage variation (e.g. sag, swell, or interruption) and possibly a modifier indicating the duration of the variation (e.g., instantaneous, momentary, or temporary).3.1.74 waveform distortion: A steady-state deviation from an ideal sine wave of power frequency princi-pally characterized by the spectral content of the deviation [B13].3.2 Avoided termsThe following terms have a varied history of usage, and some may have speciÞc deÞnitions for other appli-cations. It is an objective of this recommended practice that the following ambiguous words not be used in relation to the measurement of power quality phenomena:blackout frequency shiftblink glitchbrownout (see 4.4.3.2)interruption (when not further qualiÞed)bump outage (see 4.4.3.3)clean ground power surgeclean power raw powercomputer grade ground raw utility powercounterpoise ground shared grounddedicated ground spikedirty ground subcycle outagesdirty power surge (see 4.4.1)wink。

easYgen-2200 2300 2500 Genset Control for Multiple

easYgen-2200/2300/2500DESCRIPTIONThe easYgen-2000 Series is a compact, affordable genset control and protection package for load sharing upto 16 gensets in island operation, or parallel operation of a single unit with a utility. Its integrated load depend-ent start/stop programming allows you to define how gensets are brought on- and off-line to support changing load demands. It equally works with a mix of different sized engines, so you can maintain the spinning reserve you need while optimizing fuel efficiency.The easYgen-2000 Series works with many common industrial interfaces: CANopen for peer-to-peer load shar-ing; J1939 for engine ECU; Modbus RTU for PLC, HMI, and SCADA; and modem for remote control and pro-gramming using Woodward ToolKit software.SPECIFICATIONSPower supply .......................................................... 12/24 Vdc (8 to 40 Vdc) Intrinsic consumption .......................................max.~ 8 W (easYgen-2200) ......................................................................max..~ 12 W (easYgen-2500) Ambient temperature (operation) ....................... -20 to 70 °C / -4 to 158 °F Ambient temperature (storage) ........................ -30 to 80 °C / -22 to 176 °F Ambient humidity...................................................... 95 %, non-condensing Voltage .............................................................................................. (/∆) 120 Vac [1]Rated (V rated) ............................................ 69/120 Vac Max. value (V max) ............................................ 86/150 VacRated voltage phase – ground ............................ 150 VacSurge volt.(V surge) .................................................... 2.5 kV and 480 Vac [4]Rated (V rated) .......................................... 277/480 Vac Max. value (V max) .......................................... 346/600 VacRated voltage phase – ground ............................ 300 VacSurge volt.(V surge) .................................................... 4.0 kV Accuracy .......................................................................................... C lass 1 Linear measuring range .............................................................. 1.25×V rated Measuring frequency............................................... 50/60 Hz (40 to 85 Hz) High Impedance Input; Resistance per path ....... [1] 0.498 MΩ, [4] 2.0 MΩMax. power consumption per path ................................................ < 0.15 W Current (Isolated)Rated (I rated) .............................. [1] ../1 A or [5] ../5 A Linear measuring range ........................................................ I gen = 3.0×I ratedI mains/ground = 1.5×I rated Burden .......................................................................................... < 0.15 VA Rated short-time current (1 s) .................................[1] 50×I rated, [5] 10×I rated Discrete inputs .............................................................................. i solated Input range ............................................................. 12/24 Vdc (8 to 40 Vdc) Input resistance .............................................................. approx. 20 kOhms Relay outputs ........................................................................ p otential free Contact material ............................................................................... AgCdO Load (GP) ...................................................................... 2.00 Aac@250 Vac2.00 Adc@24 Vdc / 0.36 Adc@125 Vdc / 0.18 Adc@250 Vdc Pilot duty (PD) ..............................................................................................1.00 Adc@24 Vdc / 0.22 Adc@125 Vdc / 0.10 Adc@250 Vdc Analog inputs (none isolated)............................................ f reely scalable Type ................................................................. 0 to 500 Ohms / 0 to 20 mA Resolution ........................................................................................... 11 Bit Analog outputs (isolated)................................................... f reely scalable Type ..................................................................... ± 10 V / ± 20 mA / PWM Insulation voltage (continuously) ..................................................... 100 Vac Insulation test voltage (≤ 5s) ......................................................... 1000 Vac Resolution ................................................. 11/12 Bit (depending on output) ± 10 V (scalable) ........................................ i nternal resistance ~ 500 Ohms ± 20 mA (scalable) .............................................. m aximum load 500 Ohms Housing Front panel flush mounting ............Plastic housing Dimensions WxHxD 219 × 171 × 61 mm (easYgen-2200/2300)WxHxD .........219 × 171 × 98 mm (easYgen-2500) Front cutout WxH ........................... 186 [+1.1] × 138 [+1.0] mm Connection .................................................... s crew/plug terminals 2.5 mm² Front ................................................................................. i nsulating surface Sealing Front ........................... IP65 (with screw fastening)Front ........................... IP54 (with clamp fastening)Back ............................................................... IP20 Weight ................................................ a pprox. 800 g (easYgen-2200/2300) ................................................................. a pprox. 1,100 g (easYgen-2500) Listings....................................... U L, cUL, GOST-R (easYgen-2200/2500) Marine.............................. L R (Type Approval), ABS (Design Assessment) .................................................................................. (easYgen-2200/2500) Disturbance test (CE) .......... t ested according to applicable EN guidelinesDIMENSIONSeasYgen-2200/2300easYgen-2500TERMINAL DIAGRAMeasYgen-2200Differences between packages:easYgen-2200 P1easYgen-2200 P2easYgen-2300Differences between packages:easYgen-2300 P1easYgen-2300 P2easYgen-2500 (P1)CONTACTNorth & Central America Tel.: +1 (208) 278 3370South AmericaTel.: +55 19 3708 4800EuropeTel.: +49 711 78954 510Middle East & AfricaTel.: +971 (2) 678 4424RussiaTel.: +49 711 78954-515ChinaTel.: +86 512 8818 5515IndiaTel.: +91 124 4399 500ASEAN & OceaniaTel.: +49 711 78954 510 SALES SUPPORT✉******************************* TECHNICAL SUPPORT✉******************************* Subject to alterations, errors excepted.Subject to technical modifications. This document is distributed for informa-tional purposes only. It is not to be con-strued as creating or becoming part of any Woodward Company contractual or warranty obligation unless expressly stated in a written sales contract.We appreciate your comments about the content of our publications. Please send comments including the document num-ber below to*********************© WoodwardAll Rights Reserved37548B - 2021/08/Stuttgart FEATURES OVERVIEWMeasuringGenerator voltage (3-phase/4-wire)Generator current (3x true r.m.s.)#2 via serial (external Woodward DPC cable required – USB connector: P/N 5417-1251 / RS-232 connector: P/N 5417-557) or CAN connection by ToolKit software #3 calculated ground current#4 it is possible to connect up to two digital IO expansion boards (P/N 8440-2116), which provide 8 additional DIs and DOs each#5 a screw and a clamp kit are delivered with the unit for fastening#6 external resistor (500 Ohms) for voltage mode is part of delivery#7 Soft interchange from generator to mains but hard interchange from mains to generatorReleased。

SAE J4002-2010

3.2
H-point Travel Path ....................................................................................................................................... 6
SAE reviews each technical report at least every five years at which time it may be reaffirmed, revised, or cancelled. SAE invites your written comments and suggestions.
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Copyright © 2010 SAE International
All rights reserved. No part of this publication may be reproduced, stored in a retrieval system or transmitted, in any form or by any means, electronic, mechanical, photocopying, recording, or otherwise, without the prior written permission of SAE.

Bode and Fano Impedance Matching

2. T. Hirono, Y. Shibata, W.W. Lui, S. Seki, and Y. Yoshikuni, The second-order condition for the dielectric interface orthogonal to the Yee-lattice axis in the FDTD scheme, IEEE Microwave Guided Wave Lett 10 (2000), 359 –361.
3. K.P. Hwang and A.C. Cangellaris, Effective permittivities for secondorder accurate FDTD equations at dielectric interface, IEEE Microwave Guided Wave Lett 11 (2001), 158 –160.
© 2008 Wiley Periodicals, Inc.
BODE AND FANO IMPEDANCE MATCHING
11. D.M. Sheen, S.M. Ali, M.D. Abouzahra, and J.A. Kong, Application of the three-dimensional ﬁnite-difference time-domain method to the analysis of planar microstrip circuits, IEEE Trans. Microwave Theory Tech 38 (1990), 849 – 857.
6. Q.X. Chu and H. Ding, Second-order accurate FDTD equations at dielectric interface for TE modes, IEEE Antenna Propag Symp Dig 1 (2005), 205–208.

MPI TITAN RF Probe Selection Guide

MPI Probe Selection GuideWith a critical understanding of the numerous measurement challenges associated with today’s RF ap-plications, MPI Corporation has developed TITAN™ RF Probes, a product series specifically optimized for these complex applications centered upon the requirements of advanced RF customers.TITAN™ Probes provide the latest in technology and manufacturing advancements within the field of RF testing. They are derived from the technology transfer that accompanied the acquisition of Allstron, then significantly enhanced by MPI’s highly experienced RF testing team and subsequently produced utilizing MPI’s world class MEMS technology. Precisely manufactured, the TITAN™ Probes include matched 50 Ohm MEMS contact tips with improved probe electrical characteristics which allow the realization of unmat -ched calibration results over a wide frequency range. The patented protrusion tip design enables small passivation window bond pad probing, while significantly reducing probe skate thus providing the out -standing contact repeatability required in today’s extreme measurement environments. TITAN TM Probes with all their features are accompanied by a truly affordable price.The TITAN™ Probe series are available in single-ended and dual tip configurations, with pitch range from 50 micron to 1250 micron and frequencies from 26 GHz to 110 GHz. TITAN™ RF Probes are the ideal choice for on-wafer S-parameter measurements of RF, mm-wave devices and circuits up to 110 GHz as well as for the characterization of RF power devices requiring up to 10 Watts of continuous power. Finally, customers can benefit from both long product life and unbeatable cost of ownership which they have desired foryears.Unique design of the MEMS coplanar contacttip of the TITAN™ probe series.DC-needle-alike visibility of the contact point and the minimal paddamage due to the unique design of the tipAC2-2 Thru S11 Repeatability. Semi-Automated System.-100-80-60-40-200 S 11 E r r o r M a g n i t u d e (d B )Frequency (GHz)Another advantage of the TITAN™ probe is its superior contact repeatability, which is comparable with the entire system trace noise when measured on the semi-automated system and on gold contact pads.CROSSTALKCrosstalk of TITAN™ probes on the short and the bare ceramic open standard of 150 micron spacing compared to conventional 110 GHz probe technologies. Results are corrected by the multiline TRL calibration. All probes are of GSG configuration and 100 micron pitch.-80-60-40-200Crosstalk on Open. Multiline TRL Calibration.M a g (S21) (d B )Frequency (GHz)-80-60-40-200Crosstalk on Short. Multiline TRL Calibration.M a g (S21) (d B )Frequency (GHz)The maximal probe c ontac t repeatability error of the c alibrate S11-parameter of the AC2-2 thru standard by T110 probes. Semi-automated system. Ten contact circles.Cantilever needle material Ni alloy Body materialAl alloy Contact pressure @2 mils overtravel 20 g Lifetime, touchdowns> 1,000,000Ground and signal alignment error [1]± 3 µm [1]Planarity error [1] ± 3 µm [1]Contact footprint width < 30 µm Contact resistance on Au < 3 mΩThermal range-60 to 175 °CMechanical CharacteristicsAC2-2 Thru S21 Repeatability. Manual TS50 System.-100-80-60-40-200S 21 E r r o r M a g n i t u d e (d B )Frequency (GHz)MECHANICAL CHARACTERISTICSThe maximal probe c ontac t repeatability error of the c alibrate S21-parameter of the AC2-2 thru standard by T50 probes. Manual probe system TS50.26 GHZ PROBES FOR WIRELESS APPLICATIONSUnderstanding customer needs to reduce the cost of development and product testing for the high competitive wireless application market, MPI offers low-cost yet high-performance RF probes. The specifically developed SMA connector and its outstanding transmission of electro-magnetic waves through the probe design make these probes suitable for applications frequencies up to 26 GHz. The available pitch range is from 50 micron to 1250 micron with GS/SG and GSG probe tip configurations. TITAN™ 26 GHz probes are the ideal choice for measurement needs when developing components for WiFi, Bluetooth, and 3G/4G commercial wireless applications as well as for student education.Characteristic Impedance 50 ΩFrequency rangeDC to 26 GHz Insertion loss (GSG configuration)1< 0.4 dB Return loss (GSG configuration)1> 16 dB DC current ≤ 1 A DC voltage ≤ 100 V RF power, @10 GHz≤ 5 WTypical Electrical Characteristics26 GHz Probe Model: T26Connector SMAPitch range50 µm to 1250 µm Standard pitch step from 50 µm to 450 µm from 500 µm to 1250 µm25 µm step 50 µm stepAvailable for 90 µm pitch Tip configurations GSG, GS, SG Connector angleV-Style: 90-degree A-Style: 45-degreeMechanical CharacteristicsT26 probe, A-Style of the connectorTypical Electrical Characteristics: 26 GHz GSG probe, 250 micron pitchPROBES FOR DEVICE AND IC CHARACTERIZATION UP TO 110 GHZTITAN™ probes realize a unique combination of the micro-coaxial cable based probe technology and MEMS fabricated probe tip. A perfectly matched characteristic impedance of the coplanar probe tips and optimized signal transmission across the entire probe down to the pads of the device under test (DUT) result in excellent probe electrical characteristics. At the same time, the unique design of the probe tip provides minimal probe forward skate on any type of pad metallization material, therefo -re achieving accurate and repeatable measurement up to 110 GHz. TITAN™ probes are suitable for probing on small pads with long probe lifetime and low cost of ownership.The TITAN™ probe family contains dual probes for engineering and design debug of RF and mm-wave IC’s as well as high-end mm-wave range probes for S-parameter characterization up to 110 GHz for modeling of high-performance microwave devices.Characteristic Impedance 50 ΩFrequency rangeDC to 40 GHz Insertion loss (GSG configuration)1< 0.6 dB Return loss (GSG configuration)1> 18 dB DC current ≤ 1 A DC voltage ≤ 100 V RF power, @10 GHz≤ 5 WTypical Electrical Characteristics40 GHz Probe Model: T40Connector K (2.92 mm)Pitch range50 µm to 500 µmStandard pitch step For GSG configuration:from 50 µm to 450 µm from 500 µm to 800 µmFor GS/SG configuration:from 50 µm to 450 µm 25 µm step 50 µm stepAvailable for 90 µm pitch25 µm stepAvailable for 90/500 µm pitch Tip configurations GSG, GS, SG Connector angleV-Style: 90-degree A-Style: 45-degreeMechanical CharacteristicsTypical Electrical Characteristics: 40 GHz GSG probe, 150 micron pitchT40 probe, A-Style of the connectorCharacteristic Impedance50 ΩFrequency range DC to 50 GHz Insertion loss (GSG configuration)1< 0.6 dB Return loss (GSG configuration)1> 17 dBDC current≤ 1 ADC voltage≤ 100 VRF power, @10 GHz≤ 5 W Typical Electrical Characteristics Connector Q (2.4 mm)Pitch range50 µm to 250 µm Standard pitch stepFor GSG configuration: from 50 µm to 450 µm For GS/SG configuration: from 50 µm to 450 µm 25 µm stepAvailable for 90/500/550 µm pitch 25 µm stepAvailable for 90/500 µm pitchTip configurations GSG, GS, SG Connector angle V-Style: 90-degreeA-Style: 45-degreeMechanical CharacteristicsT50 probe, A-Style of the connectorTypical Electrical Characteristics: 50 GHz GSG probe, 150 micron pitchCharacteristic Impedance50 ΩFrequency range DC to 67 GHz Insertion loss (GSG configuration)1< 0.8 dB Return loss (GSG configuration)1> 16 dBDC current≤ 1 ADC voltage≤ 100 VRF power, @10 GHz≤ 5 W Typical Electrical Characteristics Connector V (1.85 mm)Pitch range50 µm to 250 µm Standard pitch stepFor GSG configuration: from 50 µm to 400 µm For GS/SG configuration: from 50 µm to 250 µm 25 µm step Available for 90 µm pitch25 µm step Available for 90 µm pitchTip configurations GSG Connector angle V-Style: 90-degreeA-Style: 45-degreeMechanical CharacteristicsT67 probe, A-Style of the connectorTypical Electrical Characteristics: 67 GHz GSG probe, 100 micron pitchCharacteristic Impedance 50 ΩFrequency rangeDC to 110 GHz Insertion loss (GSG configuration)1< 1.2 dB Return loss (GSG configuration)1> 14 dB DC current ≤ 1 A DC voltage ≤ 100 V RF power, @10 GHz≤ 5 WTypical Electrical CharacteristicsMechanical CharacteristicsTypical Electrical Characteristics: 110 GHz GSG probe, 100 micron pitchT110 probe, A-Style of the connectorCharacteristic impedance50 ΩFrequency range DC to 220 GHz Insertion loss (GSG configuration)1< 5 dB Connector end return loss(GSG configuration)1> 9 dBTip end return loss(GSG configuration)1> 13 dBDC current≤ 1.5 ADC voltage≤ 50 V Typical Electrical CharacteristicsConnector Broadband interface Pitch range50/75/90/100/125 µm Temperature range -40 ~ 150 ºC Contact width15 µmquadrant compatible(allowing corner pads)Yes recommended pad size20 µm x 20 µm recommended OT (overtravel)15 µmcontact resistance(on Al at 20 ºC using 15 µm OT)< 45 mΩlifetime touchdowns(on Al at 20 ºC using 15 µm OT)> 200,000Mechanical CharacteristicsT220 probe, broadband interface Typical Performance (at 20 ºC for 100 µm pitch)BODY DIMENSIONS PROBES Single-Ended V-StyleT220 GHz Probe1.161.1628.328437.455.6512.5527.73Single-Ended A-StyleCALIBRATION SUBSTRATESAC-series of calibration standard substrates offers up to 26 standard sets for wafer-level SOL T, LRM probe-tip cali -bration for GS/SG and GSG probes. Five coplanar lines provide the broadband reference multiline TRL calibration as well as accurate verification of conventional methods. Right-angled reciprocal elements are added to support the SOLR calibration of the system with the right-angled configuration of RF probes. A calibration substrate for wide-pitch probes is also available.Material Alumina Elements designCoplanarSupported calibration methods SOLT, LRM, SOLR, TRL and multiline TRL Thickness 635 µmSizeAC2-2 : 16.5 x 12.5 mm AC3 : 16.5 x 12.5 mm AC5 : 22.5 x 15 mm Effective velocity factor @20 GHz0.45Nominal line characteristic impedance @20 GHz 50 ΩNominal resistance of the load 50 ΩTypical load trimming accuracy error ± 0.3 %Open standardAu pads on substrate Calibration verification elements Yes Ruler scale 0 to 3 mm Ruler step size100 µmCalibration substrate AC2-2Probe Configuration GSGSupported probe pitch100 to 250 µm Number of SOL T standard groups 26Number of verification and calibration lines5Calibration substrate AC-3Probe Configuration GS/SG Supported probe pitch50 to 250 µm Number of SOL T standard groups 26Number of verification and calibration lines5Calibration substrate AC-5Probe Configuration GSG, GS/SG Supported probe pitch250 to 1250 µm Number of SOL T standard groups GSG : 7GS : 7SG : 7Open standardOn bare ceramic Number of verification and calibration linesGSG : 2GS : 1Typical characteristics of the coplanar line standard of AC2-2 calibration substrate measured using T110-GSG100 probes, and methods recommended by the National Institute of Standard and Technologies [2, 3].2468(d B /c m )F requency (G Hz)α-6-4-202I m a g (Z 0) ()F requency (G Hz)AC2-2 W#006 and T110A-GSG100Ω2.202.222.242.262.282.30 (u n i t l e s s )F requency (G Hz)β/βо4045505560R e a l (Z 0) ()F requency (G Hz)ΩTypical Electrical CharacteristicsMPI QAlibria® RF CALIBRATION SOFTWAREMPI QAlibria® RF calibration software has been designed to simplify complex and tedious RF system calibration tasks. By implementing a progressive disclosure methodology and realizing intuitive touch operation, QAlibria® provides crisp and clear guidance to the RF calibration process, minimizing con-figuration mistakes and helping to obtain accurate calibration results in fastest time. In addition, its concept of multiple GUI’s offers full access to all configuration settings and tweaks for advanced users. QAlibria® offers industry standard and advanced calibration methods. Furthermore, QAlibria® is integrated with the NIST StatistiCal™ calibration packages, ensuring easy access to the NIST mul-tiline TRL metrology-level calibration and uncertainty analysis.MPI Qalibria® supports a multi-language GUI, eliminating any evitable operation risks and inconvenience.SpecificationsRF AND MICROWAVE CABLESMPI offers an excellent selection of flexible cables and acces-sories for RF and mm-wave measurement applications forcomplete RF probe system integration.CablesHigh-quality cable assemblies with SMA and 3.5 mm connectorsprovide the best value for money, completing the entry-level RFsystems for measurement applications up to 26 GHz. Phase stab-le high-end flexible cable assemblies with high-precision 2.92, 2.4, 1.85 and 1 mm connectors guarantee high stability, accuracy and repeatability of the calibration and measurement for DC applications up to 110 GHz.MPI offers these cable assemblies in two standard lengths of 120 and 80 cm, matching the probe system’s footprint and the location of the VNA.Cables Ordering InformationMRC-18SMA-MF-80018 GHz SMA flex cable SMA (male) - SMA (female), 80 cmMRC-18SMA-MF-120018 GHz SMA flex cable SMA (male) - SMA (female), 120 cmMRC-26SMA-MF-80026 GHz SMA flex cable SMA (male) - SMA (female), 80 cmMRC-26SMA-MF-120026 GHz SMA flex cable SMA (male) - SMA (female), 120 cmMRC-40K-MF-80040 GHz flex cable 2.92 mm (K) connector, male-female, 80 cm longMRC-40K-MF-120040 GHz flex cable 2.92 mm (K) connector, male-female, 120 cm longMRC-50Q-MF-80050 GHz flex cable 2.4 mm (Q) connector, male-female , 80 cm longMRC-50Q-MF-120050 GHz flex cable 2.4 mm (Q) connector, male-female , 120 cm longMRC-67V-MF-80067 GHz flex cable 1.85 mm (V) connector, male-female, 80 cm longMRC-67V-MF-120067 GHz flex cable 1.85 mm (V) connector, male-female, 120 cm longMMC-40K-MF-80040 GHz precision flex cable 2.92 mm (K) connector, male-female, 80 cm long MMC-40K-MF-120040 GHz precision flex cable 2.92 mm (K) connector, male-female, 120 cm long MMC-50Q-MF-80050 GHz precision flex cable 2.4 mm (Q) connector, male-female , 80 cm long MMC-50Q-MF-120050 GHz precision flex cable 2.4 mm (Q) connector, male-female , 120 cm long MMC-67V-MF-80067 GHz precision flex cable 1.85 mm (V) connector, male-female, 80 cm long MMC-67V-MF-120067 GHz precision flex cable 1.85 mm (V) connector, male-female, 120 cm long MMC-110A-MF-250110 GHz precision flex cable 1 mm (A) connector, male-female, 25 cm longMPI Global PresenceDirect contact:Asia region: ****************************EMEA region: ******************************America region: ********************************MPI global presence: for your local support, please find the right contact here:/ast/support/local-support-worldwide© 2023 Copyright MPI Corporation. All rights reserved.[1] [2][3] REFERENCESParameter may vary depending upon tip configuration and pitch.R. B. Marks and D. F. Williams, "Characteristic impedance determination using propagation constant measu -rement," IEEE Microwave and Guided Wave Letters, vol. 1, pp. 141-143, June 1991.D. F. Williams and R. B. Marks, "Transmission line capacitance measurement," Microwave and Guided WaveLetters, IEEE, vol. 1, pp. 243-245, 1991.AdaptersHigh-In addition, high-quality RF and high-end mm-wave range adapters are offered to address challenges ofregular system reconfiguration and integration with different type of test instrumentation. MRA-NM-350F RF 11 GHz adapter N(male) - 3.5 (male), straight MRA-NM-350M RF 11 GHz adapter N(male) - 3.5 (female), straightMPA-350M-350F Precision 26 GHz adapter 3.5 mm (male) - 3.5 mm (female), straight MPA-350F-350F Precision 26 GHz adapter 3.5 mm (female) - 3.5 mm (female), straight MPA-350M-350M Precision 26 GHz adapter 3.5 mm (male) - 3.5 mm (male), straight MPA-292M-240F Precision 40 GHz adapter 2.92 mm (male) - 2.4 mm (female), straight MPA-292F-240M Precision 40 GHz adapter 2.92 mm (female) - 2.4 mm (male), straight MPA-292M-292F Precision 40 GHz adapter 2.92 mm (male) - 2.92 mm (female), straight MPA-292F-292F Precision 40 GHz adapter 2.92 mm (female) - 2.92 mm (female), straight MPA-292M-292M Precision 40 GHz adapter 2.92 mm (male) - 2.92 mm (male), straight MPA-240M-240F Precision 50 GHz adapter 2.4 mm (male) - 2.4 mm (female), straight MPA-240F-240F Precision 50 GHz adapter 2.4 mm (female) - 2.4 mm (female), straight MPA-240M-240M Precision 50 GHz adapter 2.4 mm (male) - 2.4 mm (male), straight MPA-185M-185F Precision 67 GHz adapter 1.85 mm (male) -1.85 mm (female), straight MPA-185F-185F Precision 67 GHz adapter 1.85 mm (female) -1.85 mm (female), straight MPA-185M-185M Precision 67 GHz adapter 1.85 mm (male) -1.85 mm (male), straight MPA-185M-100FPrecision 67 GHz adapter 1.85 mm (male) -1.00 mm (female), straightDisclaimer: TITAN Probe, QAlibria are trademarks of MPI Corporation, Taiwan. StatistiCal is a trademark of National Institute of Standards and Technology (NIST), USA. All other trademarks are the property of their respective owners. Data subject to change without notice.。

哈工大博士学位论文模板

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LATEX TEMPLATE FOR MASTER/DOCTOR THESIS/DISSERTATION OF HARBIN INSTITUTE OF TECHNOLOGY
Candidate: Supervisor: Academic Degree Applied for: Specialty: Affiliation: Date of Defense: Degree-Conferring-Institution:

Adaptive tracking control of uncertain MIMO nonlinear systems with input constraints

article
info
abstract
In this paper, adaptive tracking control is proposed for a class of uncertain multi-input and multi-output nonlinear systems with non-symmetric input constraints. The auxiliary design system is introduced to analyze the effect of input constraints, and its states are used to adaptive tracking control design. The spectral radius of the control coefficient matrix is used to relax the nonsingular assumption of the control coefficient matrix. Subsequently, the constrained adaptive control is presented, where command filters are adopted to implement the emulate of actuator physical constraints on the control law and virtual control laws and avoid the tedious analytic computations of time derivatives of virtual control laws in the backstepping procedure. Under the proposed control techniques, the closed-loop semi-global uniformly ultimate bounded stability is achieved via Lyapunov synthesis. Finally, simulation studies are presented to illustrate the effectiveness of the proposed adaptive tracking control. © 2011 Elsevier Ltd. All rights reserved.

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Examiners' Report - Paper D 2010 - Part IIIn this year's paper there were not so many applications or inventions. Hence, the analysis phase was relatively straightforward, but the candidates had to define important strategies and actions in order to accommodate the client's needs.The analysis of the existing situation and the application of legal provisions (for example the steps to request further processing) was generally answered well. However, to achieve good marks it was also necessary to recognise and propose actions that correspond best to the client's requirements.The main points in this year's paper were the following:1. In the first part it had to be recognised that EPKM does not disclose the structure ofthe signal necessary for carrying out the fishing method because it only refers to EP1.Therefore, KA could render EPKM unpatentable due to a lack of sufficient disclosure by withdrawing EP1 before publication. It had also to be realised that priority fromEP1 should not be claimed because then EP1 would be made publicly available with the publication of EP3 (as the priority document in the file of EP3) with theconsequence that the fishing method in EPKM would then be sufficiently disclosed.Additionally, it was important to spot that the disclosure of the fishing method at the website of KM would, in combination with the structure of the signal as disclosed in EP3, stop any future patenting of the method.2. In improving KA's patent situation in Europe, patent rights from EP3 were necessary.The report of KA became prior art when the filing date of EP3 was changed, so it was vital to restore the original filing date of EP3 and claim priority from EP2. Most of the candidates recognised this and proposed the correct procedure to achieve it, i.e.adding a claim to priority from EP2 in EP3 and using the priority document to file the missing parts (under Rule 56(3) EPC) so that the filing date would not be changed.However, the first step to take was to withdraw the already submitted missing parts as an answer to the communication of the EPO.3. In helping Norwayfish against Swedishfish, most of the candidates recognised thatthe disclosure of EP4 was too general to be novelty destroying against EPF and that PCTJU could be used for a novelty objection in an opposition against EPF. Most of the candidates also recognised that it was still possible to enter the Europeanregional phase of PCTJU through further processing and the majority proposed the correct series of steps to take. In order to answer the question correctly it wasnecessary to realise that due to the fact that the EPC entered into force in Norwayonly on 01.01.2008, Norway was designated in EPF but not in EP4, nor was itincluded in the EP designation of PCTJU (EP-PCT JU). However, under EPC2000, EP- PCTJU would be prior art for all contracting states (EPF filed after 12/2007, EPC 2000 applies for examination and opposition procedures concerning EPF).It is noted that candidates who proposed on the basis of Art 153 (4) EPC and Rule165 EPC that it was only necessary to request further processing for payment of the EP filing fee and for filing a translation for PCT-JU in order to make it prior art under Art. 54(3) EPC did not lose marks.4. In order to use patent rights against Swedishfish, which has all its activities in Norway,the client must have patent rights in Norway .Attention had to be paid to the fundamental issue of checking the countries in which EP4, PCTJU or EPF may be enforced, thereby realising that, for the reasonsmentioned above, Norway could not be designated in EP4 nor in EP-PCTJU.As a consequence, KA had no patent rights in Norway that could be used to attack Swedishfish. It should, however, be investigated whether an entry into Norwegiannational directly from PCTJU might be possible. Finally, with EPF revoked and noother patent rights existing in Norway, the use of material M would be free there.Possible Solution - Paper D 2010 - Part II1. Stopping KM and everyone else from having a patent for the fishing method (14 marks)EP1 is the first filing for the signal attracting only adult fish. EPKM is the first filing for the fishing method using this signal.The public conference and the video presented there are state of the art against EPKM, but since the characteristics of the signal were not disclosed in the video they do not constitute an enabling disclosure and cannot be considered as relevant prior art.EPKM discloses the use of the signal for a fishing method, but it does not disclose the characteristics of the signal necessary to carry out the fishing method since it makes only a reference to EP1. For the fishing method claimed in EPKM to be sufficiently disclosed, EP1 must be available at the EPO on the filing date of EPKM (which is the case) and EP1 must be available to the public on or before the date of publication of EPKM.EP1 has not been published yet. If publication of EP1 is avoided, then the fishing method of EPKM would be insufficiently disclosed and therefore not patentable. It is possible to withdraw EP1 before publication. Publication of EP1 will be in July 2010, so there are still about 2 months left before the termination of the technical preparations (5 weeks before publication). EP1 should be withdrawn within this time frame so that it will be certain that it will not be published. In addition, no priority should be claimed from EP1 for any further European patent application (eg.EP2, EP3) because after publication of that further application, which would take place in July 2010 (18 months from priority), the priority document, i.e. EP1, would be also available to the public as part of the file.As referenced document EP1 will not be available to the public, EPKM will suffer from insufficiency of disclosure regarding the fishing method which will not be patentable. There are alternative courses of action at this point: KA could inform KM that their application would not be patentable as far as the fishing method is concerned in the hope that they will withdraw or abandon it or, in the case that EPKM is granted by the EPO, opposition can be filed against EPKM on the ground of lack of sufficiency of disclosure.Moreover, the publication of the content of EPKM at the KM website on the day after EPKM's filing or the publication of EPKM itself in combination with the publication of the structure and the characteristics of the signal in the report of KA at the end of January 2010 will be enabling prior art against any future application related to the fishing method.2. Improving KA's patent situation in Europe (23 marks)EP2 is the first application disclosing the filter F1 and the circuit C1, but the disclosure of the circuit C1 is not enabling. EP3 is the first enabling disclosure of C1 and the inventive connection between C and F1.The public conference and the video on January 20, 2009 cannot be used as prior art against EP2 or EP3 because the characteristics of the signal or the circuits to produce it were not disclosed and no enabling disclosure of the signal took place.When/if EPKM is published it would be a prior art document relevant only for novelty (Art. 54(3) document) against EP2 and EP3, but not relevant because it does not disclose the nature of the signal or the circuit to produce it.EP2 when/if published will be prior art document under 54(3) EPC relevant only for novelty against claims 1 and 2 of EP3.EP2 can give KA protection for the filter F1 and the signal but not for the circuit C1 since it is not sufficiently disclosed. Hence, the only way KA can get protection for C1 is via EP3. However, EP3 has had its filing date moved to 02.02.2010 after the submission of the missing parts. The report of KA with EP3 was made available to the public in the library, even if nobody consulted it, as of end of January 2010. The report will thus be novelty destroying for EP3 with the new date of filing. In order for KA to be able to get protection via EP3, it is necessary for EP3 to have a filing/priority date before the end of January 2010.It is possible to recover the original filing date of EP3.Your request for correction dated 02.02.2010 should be withdrawn to avoid the change of the filing date. This can be done within 1 month after notification of the communication under R56 EPC, i.e. until 27.03.2010, extended to 29.03.2010. Then EP3 will have a filing date before the publication of the report and the report will not be prior art anymore.It is necessary to introduce the missing parts for sufficiency of disclosure of EP3. This is possible by claiming the priority of EP2 and requesting their introduction without changing the filing date.EP3 was filed within 12 months from the filing date of EP2 which ended on 01.03.2010. A priority claim can be added until 16 months from the priority date, i.e. 01.07.2010 (according to Rule 52 EPC).KA must request the addition of a claim to the priority of EP2 in EP3 and request correction (according to Rule 56(3) EPC) in order to introduce the missing pages 6 - 9. Request for correction is still possible until 12.03.2010 (i.e. 2 months from filing of EP3). Therefore, the withdrawal of the missing parts according to your request for correction dated 02.02.2010 has to be made before 12.03.2010, you can not wait until 29.03.2010. Neither can you wait for 01.07.2010 to add priority claim.Claims to an underwater camera comprising the circuit C1 and the inventive connection between F1 and C could be added in EP3 or in a possible divisional patent application. 3. Helping Norwayfish (NF) in their conflict with Swedishfish (SF) (19 marks)EPF validly claims priority from S1, therefore the effective date of EPF is in October 2007. EP4 is prior art document under Art. 54(3) EPC against EPF. Since EP4 does not disclose material M but only the general class G, EPF is new over EP4.The only document which discloses material M is PCTJU. If PCTJU validly enters the European regional (EP) phase, it would be prior art document under Art. 54(3) EPCagainst EPF. KA should accept the offer of JU and have the patent rights of PCTJU transferred to them.The time limit for PCTJU to enter EP phase (31 months from filing) ended in December 2009. It is still possible to ask for further processing which should be done within 2 months from the notification of the communication of loss of rights. The two months end on14.03.2010, extended to 15.03.2010. With the request for further processing, all the acts due for entry into the EP phase should be completed and the fee for further processing should be paid, for each omitted act.[Pursuant to Art. 153 and Rule 165 EPC it appears sufficient to create prior art under Art. 54(3) EPC if the translation of PCTJU is submitted, the filing fee and the respective further processing fees are paid. However, it is advisable in the present case to complete all omitted acts to enter the EP phase to make sure that the application is published given the fact that without compliance with the requirements of Rule 159 EPC the application is deemed to be withdrawn as from expiry of the 31 months' time limit.]In order to enter the EP phase after the expiry of the 31 months time limit, KA and JU can act as joint applicants but must act via a professional representative. Alternatively, if the transfer of rights takes place before the entry in EP phase, KA can act alone but they must request the registration of the transfer at the EPO upon entry.Since EP-PCTJU has become prior art under Art. 54(3) EPC, an opposition should be filed against EPF based on lack of novelty. The time limit to file opposition against EPF ends on 09.06.2010.EPF was filed after January 2008 and therefore is deemed to designate Norway, since Norway acceded to the EPC on 01.01.2008. PCTJU on the other hand, was filed before January 2008 and therefore EP-PCTJU cannot designate Norway.However, (EPC 2000 applies and) EP-PCTJU will be a prior art document under Art. 54(3) EPC against EPF for all contracting states, so EPF will be revoked and SF will lose the protection rights of EPF in all EPC states, including Norway. With EPF revoked, the infringement proceedings against NF should not be successful.4. Using patent rights against Swedishfish (SF) (4 marks)EP4 was also filed before January 2008 and cannot designate Norway.SF has all its activities based in Norway, therefore we can use rights against SF only if we have patent rights in Norway. Neither EP4 nor EP-PCTJU would give rights in Norway and NF cannot use them against SF.PCTJU had designated Norway and could have entered the Norwegian national phase directly. However, the time limit to enter the Norwegian national phase has expired. It should be investigated whether it is still possible to enter the Norwegian national phase now. If it is possible to enter Norwegian phase of PCTJU then KA will have a Norwegian patent covering material M; SF will be infringing this patent and could be sued/stopped. If it is not possible anymore to enter the Norwegian national phase of PCTJU then the use of material M in Norway will be free for everybody after the revocation of EPF since there will be no patent right protecting it.EP4 and EP-PCTJU could be used as prior right against S1, depending on Swedish law.30 June 2010Examination Committee III agrees on .......... marks and recommends the following grade to the Examination Board:COMPENSABLE FAIL (45-49)FAIL (0-44)PASS (50-100)Candidate No.Paper D 2010 - Marking Sheet EXAMINATION COMMITTEE IIIChairman of Examination Committee III __________________________________________Maximumpossible Marker MarkerMarks awarded Question 1Question 2Question 3Question 4Question 5Question 6Question 7Question 8Question 9455445454Question 1Question 2Question 3Question 41423194Total Part I + II 100Part I Part II。