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- EMDB-71721: CryoEM reconstruction of HUWE1-USP7 complex in the closed state -

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Basic information

Entry
Database: EMDB / ID: EMD-71721
TitleCryoEM reconstruction of HUWE1-USP7 complex in the closed state
Map dataComposite HUWE1-USP7 map, unsharpened
Sample
  • Complex: HUWE1-USP7 complex
    • Protein or peptide: E3 ubiquitin-protein ligase HUWE1
    • Protein or peptide: Ubiquitin carboxyl-terminal hydrolase 7
KeywordsComplex / E3-ligase-DUB / LIGASE
Function / homology
Function and homology information


negative regulation of peroxisome proliferator activated receptor signaling pathway / regulation of telomere capping / histone ubiquitin ligase activity / negative regulation of mitochondrial fusion / regulation of establishment of protein localization to telomere / monoubiquitinated protein deubiquitination / protein branched polyubiquitination / regulation of retrograde transport, endosome to Golgi / positive regulation of type 2 mitophagy / DNA alkylation repair ...negative regulation of peroxisome proliferator activated receptor signaling pathway / regulation of telomere capping / histone ubiquitin ligase activity / negative regulation of mitochondrial fusion / regulation of establishment of protein localization to telomere / monoubiquitinated protein deubiquitination / protein branched polyubiquitination / regulation of retrograde transport, endosome to Golgi / positive regulation of type 2 mitophagy / DNA alkylation repair / deubiquitinase activity / HECT-type E3 ubiquitin transferase / K48-linked deubiquitinase activity / regulation of tumor necrosis factor-mediated signaling pathway / symbiont-mediated disruption of host cell PML body / : / ubiquitin-ubiquitin ligase activity / negative regulation of gene expression via chromosomal CpG island methylation / Golgi organization / negative regulation of gluconeogenesis / protein monoubiquitination / protein deubiquitination / negative regulation of TORC1 signaling / protein K48-linked ubiquitination / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / transcription-coupled nucleotide-excision repair / regulation of signal transduction by p53 class mediator / positive regulation of protein ubiquitination / Regulation of PTEN localization / antiviral innate immune response / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / circadian regulation of gene expression / regulation of protein stability / base-excision repair / PML body / regulation of circadian rhythm / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / protein polyubiquitination / ubiquitin-protein transferase activity / p53 binding / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / Regulation of TP53 Degradation / ubiquitin protein ligase activity / rhythmic process / Antigen processing: Ubiquitination & Proteasome degradation / chromosome / nuclear membrane / secretory granule lumen / ficolin-1-rich granule lumen / ubiquitin-dependent protein catabolic process / membrane fusion / proteasome-mediated ubiquitin-dependent protein catabolic process / positive regulation of canonical NF-kappaB signal transduction / cell differentiation / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / nuclear body / protein stabilization / Ub-specific processing proteases / protein ubiquitination / Golgi membrane / cysteine-type endopeptidase activity / Neutrophil degranulation / protein-containing complex / mitochondrion / proteolysis / DNA binding / RNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
HUWE1, UBA domain / E3 ubiquitin ligase, domain of unknown function DUF908 / E3 ubiquitin ligase, domain of unknown function DUF913 / Domain of Unknown Function (DUF908) / Domain of Unknown Function (DUF913) / WWE domain / UBA-like domain / Ubiquitin carboxyl-terminal hydrolase 7, ICP0-binding domain / ICP0-binding domain of Ubiquitin-specific protease 7 / Ubiquitin carboxyl-terminal hydrolase, C-terminal ...HUWE1, UBA domain / E3 ubiquitin ligase, domain of unknown function DUF908 / E3 ubiquitin ligase, domain of unknown function DUF913 / Domain of Unknown Function (DUF908) / Domain of Unknown Function (DUF913) / WWE domain / UBA-like domain / Ubiquitin carboxyl-terminal hydrolase 7, ICP0-binding domain / ICP0-binding domain of Ubiquitin-specific protease 7 / Ubiquitin carboxyl-terminal hydrolase, C-terminal / Ubiquitin-specific protease C-terminal / WWE domain superfamily / WWE domain / WWE domain profile. / HUWE1/Rev1, ubiquitin binding region / Ubiquitin binding region / MATH domain / Ubiquitin-binding motif (UBM) domain profile. / : / : / MATH/TRAF domain / MATH/TRAF domain profile. / meprin and TRAF homology / TRAF-like / HECT domain / HECT, E3 ligase catalytic domain / HECT-domain (ubiquitin-transferase) / HECT domain profile. / Domain Homologous to E6-AP Carboxyl Terminus with / Ubiquitin specific protease (USP) domain signature 2. / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Ubiquitin associated domain / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / UBA-like superfamily / Papain-like cysteine peptidase superfamily / Armadillo-type fold
Similarity search - Domain/homology
E3 ubiquitin-protein ligase HUWE1 / Ubiquitin C-terminal hydrolase 7
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.88 Å
AuthorsYatskevich S / Juszkiewicz S
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Molecular mechanism of HUWE1-HAPSTR1-USP7-mediated ubiquitin chain amplification on nuclear proteins
Authors: Yatskevich S
History
DepositionJul 16, 2025-
Header (metadata) releaseJul 22, 2026-
Map releaseJul 22, 2026-
UpdateJul 22, 2026-
Current statusJul 22, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_71721.png

Downloads & links

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Map

FileReleased
AnnotationComposite HUWE1-USP7 map, unsharpened
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.73 Å/pix.
x 380 pix.
= 277.78 Å		0.73 Å/pix.
x 380 pix.
= 277.78 Å		0.73 Å/pix.
x 380 pix.
= 277.78 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.731 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0188
Minimum - Maximum-0.20499146 - 0.5158171
Average (Standard dev.)0.0009937527 (±0.01450414)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions380380380
Spacing380380380
CellA=B=C: 277.78 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Composite HUWE1-USP7 map, sharpened

Fileemd_71721_additional_1.map
AnnotationComposite HUWE1-USP7 map, sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement of USP7 Ubl12 domain, unsharpened

Fileemd_71721_additional_2.map
AnnotationFocused refinement of USP7 Ubl12 domain, unsharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement of USP7 Ubl12 domain, sharpened

Fileemd_71721_additional_3.map
AnnotationFocused refinement of USP7 Ubl12 domain, sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement of USP7 Ubl45 domain, unsharpened

Fileemd_71721_additional_4.map
AnnotationFocused refinement of USP7 Ubl45 domain, unsharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement of USP7 Ubl45 domain, sharpened

Fileemd_71721_additional_5.map
AnnotationFocused refinement of USP7 Ubl45 domain, sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement of USP7 catalytic domain, unsharpened

Fileemd_71721_additional_6.map
AnnotationFocused refinement of USP7 catalytic domain, unsharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Focused refinement of USP7 catalytic domain, sharpened

Fileemd_71721_additional_7.map
AnnotationFocused refinement of USP7 catalytic domain, sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Consensus HUWE1-USP7 reconstruction, unsharpened

Fileemd_71721_additional_8.map
AnnotationConsensus HUWE1-USP7 reconstruction, unsharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: Consensus HUWE1-USP7 reconstruction, sharpened

Fileemd_71721_additional_9.map
AnnotationConsensus HUWE1-USP7 reconstruction, sharpened
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : HUWE1-USP7 complex

EntireName: HUWE1-USP7 complex
Components
  • Complex: HUWE1-USP7 complex
    • Protein or peptide: E3 ubiquitin-protein ligase HUWE1
    • Protein or peptide: Ubiquitin carboxyl-terminal hydrolase 7

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Supramolecule #1: HUWE1-USP7 complex

SupramoleculeName: HUWE1-USP7 complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: E3 ubiquitin-protein ligase HUWE1

MacromoleculeName: E3 ubiquitin-protein ligase HUWE1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: HECT-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 482.424406 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR FDGILADAGQ TVENMSWMLV CDRPEREQL KMLLLAVLNF TALLIEYSFS RHLYSSIEHL TTLLASSDMQ VVLAVLNLLY VFSKRSNYIT RLGSDKRTPL L TRLQHLAE ...String:
MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR FDGILADAGQ TVENMSWMLV CDRPEREQL KMLLLAVLNF TALLIEYSFS RHLYSSIEHL TTLLASSDMQ VVLAVLNLLY VFSKRSNYIT RLGSDKRTPL L TRLQHLAE SWGGKENGFG LAECCRDLHM MKYPPSATTL HFEFYADPGA EVKIEKRTTS NTLHYIHIEQ LDKISESPSE IM ESLTKMY SIPKDKQMLL FTHIRLAHGF SNHRKRLQAV QARLHAISIL VYSNALQESA NSILYNGLIE ELVDVLQITD KQL MEIKAA SLRTLTSIVH LERTPKLSSI IDCTGTASYH GFLPVLVRNC IQAMIDPSMD PYPHQFATAL FSFLYHLASY DAGG EALVS CGMMEALLKV IKFLGDEQDQ ITFVTRAVRV VDLITNLDMA AFQSHSGLSI FIYRLEHEVD LCRKECPFVI KPKIQ RPNT TQEGEEMETD MDGVQCIPQR AALLKSMLNF LKKAIQDPAF SDGIRHVMDG SLPTSLKHII SNAEYYGPSL FLLATE VVT VFVFQEPSLL SSLQDNGLTD VMLHALLIKD VPATREVLGS LPNVFSALCL NARGLQSFVQ CQPFERLFKV LLSPDYL PA MRRRRSSDPL GDTASNLGSA VDELMRHQPT LKTDATTAII KLLEEICNLG RDPKYICQKP SIQKADGTAT APPPRSNH A AEEASSEDEE EEEVQAMQSF NSTQQNETEP NQQVVGTEER IPIPLMDYIL NVMKFVESIL SNNTTDDHCQ EFVNQKGLL PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV LQEGLLQLDS ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQA TPLLHALTAA HAYIMMFVHT CRVGQSEIRS ISVNQWGSQL GLSVLSKLSQ LYCSLVWEST VLLSLCTPNS L PSGCEFGQ ADMQKLVPKD EKAGTTQGGK RSDGEQDGAA GSMDASTQGL LEGIGLDGDT LAPMETDEPT ASDSKGKSKI TP AMAARIK QIKPLLSASS RLGRALAELF GLLVKLCVGS PVRQRRSHHA ASTTTAPTPA ARSTASALTK LLTKGLSWQP PPY TPTPRF RLTFFICSVG FTSPMLFDER KYPYHLMLQK FLCSGGHNAL FETFNWALSM GGKVPVSEGL EHSDLPDGTG EFLD AWLML VEKMVNPTTV LESPHSLPAK LPGGVQNFPQ FSALRFLVVT QKAAFTCIKN LWNRKPLKVY GGRMAESMLA ILCHI LRGE PVIRERLSKE KEGSRGEEDT GQEEGGSRRE PQVNQQQLQQ LMDMGFTREH AMEALLNTST MEQATEYLLT HPPPIM GGV VRDLSMSEED QMMRAIAMSL GQDIPMDQRA ESPEEVACRK EEEERKAREK QEEEEAKCLE KFQDADPLEQ DELHTFT DT MLPGCFHLLD ELPDTVYRVC DLIMTAIKRN GADYRDMILK QVVNQVWEAA DVLIKAALPL TTSDTKTVSE WISQMATL P QASNLATRIL LLTLLFEELK LPCAWVVESS GILNVLIKLL EVVQPCLQAA KEQKEVQTPK WITPVLLLID FYEKTAISS KRRAQMTKYL QSNSNNWRWF DDRSGRWCSY SASNNSTIDS AWKSGETSVR FTAGRRRYTV QFTTMVQVNE ETGNRRPVML TLLRVPRLN KNSKNSNGQE LEKTLEESKE MDIKRKENKG NDTPLALEST NTEKETSLEE TKIGEILIQG LTEDMVTVLI R ACVSMLGV PVDPDTLHAT LRLCLRLTRD HKYAMMFAEL KSTRMILNLT QSSGFNGFTP LVTLLLRHII EDPCTLRHTM EK VVRSAAT SGAGSTTSGV VSGSLGSREI NYILRVLGPA ACRNPDIFTE VANCCIRIAL PAPRGSGTAS DDEFENLRIK GPN AVQLVK TTPLKPSPLP VIPDTIKEVI YDMLNALAAY HAPEEADKSD PKPGVMTQEV GQLLQDMGDD VYQQYRSLTR QSSD FDTQS GFSINSQVFA ADGASTETSA SGTSQGEAST PEESRDGKKD KEGDRASEEG KQKGKGSKPL MPTSTILRLL AELVR SYVG IATLIANYSY TVGQSELIKE DCSVLAFVLD HLLPHTQNAE DKDTPALARL FLASLAAAGS GTDAQVALVN EVKAAL GRA LAMAESTEKH ARLQAVMCII STIMESCPST SSFYSSATAK TQHNGMNNII RLFLKKGLVN DLARVPHSLD LSSPNMA NT VNAALKPLET LSRIVNQPSS LFGSKSASSK NKSEQDAQGA SQDSSSNQQD PGEPGEAEVQ EEDHDVTQTE VADGDIMD G EAETDSVVIA GQPEVLSSQE MQVENELEDL IDELLERDGG SGNSTIIVSR SGEDESQEDV LMDEAPSNLS QASTLQANR EDSMNILDPE DEEEHTQEED SSGSNEDEDD SQDEEEEEEE DEEDDQEDDE GEEGDEDDDD DGSEMELDED YPDMNASPLV RFERFDRED DLIIEFDNMF SSATDIPPSP GNIPTTHPLM VRHADHSSLT LGSGSSTTRL TQGIGRSQRT LRQLTANTGH T IHVHYPGN RQPNPPLILQ RLLGPSAAAD ILQLSSSLPL QSRGRARLLV GNDDVHIIAR SDDELLDDFF HDQSTATSQA GT LSSIPTA LTRWTEECKV LDAESMHDCV SVVKVSIVNH LEFLRDEELE ERREKRRKQL AEEETKITDK GKEDKENRDQ SAQ CTASKS NDSTEQNLSD GTPMPDSYPT TPSSTDAATS ESKETLGTLQ SSQQQPTLPT PPALGEVPQE LQSPAGEGGS STQL LMPVE PEELGPTRPS GEAETTQMEL SPAPTITSLS PERAEDSDAL TAVSSQLEGS PMDTSSLASC TLEEAVGDTS AAGSS EQPR AGSSTPGDAP PAVAEVQGRS DGSGESAQPP EDSSPPASSE SSSTRDSAVA ISGADSRGIL EEPLPSTSSE EEDPLA GIS LPEGVDPSFL AALPDDIRRE VLQNQLGIRP PTRTAPSTNS SAPAVVGNPG VTEVSPEFLA ALPPAIQEEV LAQQRAE QQ RRELAQNASS DTPMDPVTFI QTLPSDLRRS VLEDMEDSVL AVMPPDIAAE AQALRREQEA RQRQLMHERL FGHSSTSA L SAILRSPAFT SRLSGNRGVQ YTRLAVQRGG TFQMGGSSSH NRPSGSNVDT LLRLRGRLLL DHEALSCLLV LLFVDEPKL NTSRLHRVLR NLCYHAQTRH WVIRSLLSIL QRSSESELCI ETPKLTTSEE KGKKSSKSCG SSSHENRPLD LLHKMESKSS NQLSWLSVS MDAALGCRTN IFQIQRSGGR KHTEKHASGG STVHIHPQAA PVVCRHVLDT LIQLAKVFPS HFTQQRTKET N CESDRERG NKACSPCSSQ SSSSGICTDF WDLLVKLDNM NVSRKGKNSV KSVPVSAGGE GETSPYSLEA SPLGQLMNML SH PVIRRSS LLTEKLLRLL SLISIALPEN KVSEAQANSG SGASSTTTAT STTSTTTTTA ASTTPTPPTA PTPVTSAPAL VAA TAISTI VVAASTTVTT PTTATTTVSI SPTTKGSKSP AKVSDGGSSS TDFKMVSSGL TENQLQLSVE VLTSHSCSEE GLED AANVL LQLSRGDSGT RDTVLKLLLN GARHLGYTLC KQIGTLLAEL REYNLEQQRR AQCETLSPDG LPEEQPQTTK LKGKM QSRF DMAENVVIVA SQKRPLGGRE LQLPSMSMLT SKTSTQKFFL RVLQVIIQLR DDTRRANKKA KQTGRLGSSG LGSASS IQA AVRQLEAEAD AIIQMVREGQ RARRQQQAAT SESSQSEASV RREESPMDVD QPSPSAQDTQ SIASDGTPQG EKEKEER PP ELPLLSEQLS LDELWDMLGE CLKELEESHD QHAVLVLQPA VEAFFLVHAT ERESKPPVRD TRESQLAHIK DEPPPLSP A PLTPATPSSL DPFFSREPSS MHISSSLPPD TQKFLRFAET HRTVLNQILR QSTTHLADGP FAVLVDYIRV LDFDVKRKY FRQELERLDE GLRKEDMAVH VRRDHVFEDS YRELHRKSPE EMKNRLYIVF EGEEGQDAGG LLREWYMIIS REMFNPMYAL FRTSPGDRV TYTINPSSHC NPNHLSYFKF VGRIVAKAVY DNRLLECYFT RSFYKHILGK SVRYTDMESE DYHFYQGLVY L LENDVSTL GYDLTFSTEV QEFGVCEVRD LKPNGANILV TEENKKEYVH LVCQMRMTGA IRKQLAAFLE GFYEIIPKRL IS IFTEQEL ELLISGLPTI DIDDLKSNTE YHKYQSNSIQ IQWFWRALRS FDQADRAKFL QFVTGTSKVP LQGFAALEGM NGI QKFQIH RDDRSTDRLP SAHTCFNQLD LPAYESFEKL RHMLLLAIQE CSEGFGLA

UniProtKB: E3 ubiquitin-protein ligase HUWE1

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Macromolecule #2: Ubiquitin carboxyl-terminal hydrolase 7

MacromoleculeName: Ubiquitin carboxyl-terminal hydrolase 7 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: ubiquitinyl hydrolase 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 128.472766 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD GHNTAEEDME DDTSWRSEAT FQFTVERFSR LSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL QCNAESDSTS WSCHAQAVLK IINYRDDEKS FSRRISHLFF H KENDWGFS ...String:
MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD GHNTAEEDME DDTSWRSEAT FQFTVERFSR LSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL QCNAESDSTS WSCHAQAVLK IINYRDDEKS FSRRISHLFF H KENDWGFS NFMAWSEVTD PEKGFIDDDK VTFEVFVQAD APHGVAWDSK KHTGYVGLKN QGATCYMNSL LQTLFFTNQL RK AVYMMPT EGDDSSKSVP LALQRVFYEL QHSDKPVGTK KLTKSFGWET LDSFMQHDVQ ELCRVLLDNV ENKMKGTCVE GTI PKLFRG KMVSYIQCKE VDYRSDRRED YYDIQLSIKG KKNIFESFVD YVAVEQLDGD NKYDAGEHGL QEAEKGVKFL TLPP VLHLQ LMRFMYDPQT DQNIKINDRF EFPEQLPLDE FLQKTDPKDP ANYILHAVLV HSGDNHGGHY VVYLNPKGDG KWCKF DDDV VSRCTKEEAI EHNYGGHDDD LSVRHCTNAY MLVYIRESKL SEVLQAVTDH DIPQQLVERL QEEKRIEAQK RKERQE AHL YMQVQIVAED QFCGHQGNDM YDEEKVKYTV FKVLKNSSLA EFVQSLSQTM GFPQDQIRLW PMQARSNGTK RPAMLDN EA DGNKTMIELS DNENPWTIFL ETVDPELAAS GATLPKFDKD HDVMLFLKMY DPKTRSLNYC GHIYTPISCK IRDLLPVM C DRAGFIQDTS LILYEEVKPN LTERIQDYDV SLDKALDELM DGDIIVFQKD DPENDNSELP TAKEYFRDLY HRVDVIFCD KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF KSQGYRDGPG NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFE NRRSFKCIWL NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGEKASGKL RLLEIVSYKI IGVHQEDELL E CLSPATSR TFRIEEIPLD QVDIDKENEM LVTVAHFHKE VFGTFGIPFL LRIHQGEHFR EVMKRIQSLL DIQEKEFEKF KF AIVMMGR HQYINEDEYE VNLKDFEPQP GNMSHPRPWL GLDHFNKAPK RSRYTYLEKA IKIHN

UniProtKB: Ubiquitin C-terminal hydrolase 7

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.2 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

7jq9

Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.88 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 118192
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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