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- EMDB-41142: APC/C-CDH1-UBE2C-UBE2S-Ubiquitin-CyclinB -

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Basic information

Entry
Database: EMDB / ID: EMD-41142
TitleAPC/C-CDH1-UBE2C-UBE2S-Ubiquitin-CyclinB
Map data
Sample
  • Complex: Anaphase-Promoting Complex/Cyclosome in complex with CDH1, UBE2C, UBE2S, Cyclin-B
    • Protein or peptide: x 18 types
  • Ligand: x 1 types
KeywordsE3 RING Ligase / Ubiquitin Ligase / APC/C / Anaphase-Promoting Complex-Cyclosome / Cell Cycle / Cullin-RING ligase / LIGASE
Function / homology
Function and homology information


cyclin B1-CDK1 complex / positive regulation of mitochondrial ATP synthesis coupled electron transport / Mitotic Prophase / positive regulation of anaphase-promoting complex-dependent catabolic process / G2/M DNA replication checkpoint / Depolymerization of the Nuclear Lamina / E2F-enabled inhibition of pre-replication complex formation / positive regulation of exit from mitosis / MASTL Facilitates Mitotic Progression / positive regulation of attachment of spindle microtubules to kinetochore ...cyclin B1-CDK1 complex / positive regulation of mitochondrial ATP synthesis coupled electron transport / Mitotic Prophase / positive regulation of anaphase-promoting complex-dependent catabolic process / G2/M DNA replication checkpoint / Depolymerization of the Nuclear Lamina / E2F-enabled inhibition of pre-replication complex formation / positive regulation of exit from mitosis / MASTL Facilitates Mitotic Progression / positive regulation of attachment of spindle microtubules to kinetochore / regulation of meiotic nuclear division / protein K27-linked ubiquitination / free ubiquitin chain polymerization / positive regulation of synapse maturation / Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase / protein K29-linked ubiquitination / regulation of mitotic cell cycle spindle assembly checkpoint / protein branched polyubiquitination / Inactivation of APC/C via direct inhibition of the APC/C complex / APC/C:Cdc20 mediated degradation of mitotic proteins / Activation of NIMA Kinases NEK9, NEK6, NEK7 / Phosphorylation of Emi1 / patched binding / anaphase-promoting complex / Aberrant regulation of mitotic exit in cancer due to RB1 defects / regulation of meiotic cell cycle / anaphase-promoting complex-dependent catabolic process / metaphase/anaphase transition of mitotic cell cycle / lens fiber cell differentiation / positive regulation of synaptic plasticity / Transcriptional regulation by RUNX2 / (E3-independent) E2 ubiquitin-conjugating enzyme / regulation of exit from mitosis / anaphase-promoting complex binding / Nuclear Pore Complex (NPC) Disassembly / Phosphorylation of the APC/C / mitotic cell cycle phase transition / outer kinetochore / positive regulation of mitotic metaphase/anaphase transition / protein K6-linked ubiquitination / ubiquitin ligase activator activity / positive regulation of ubiquitin protein ligase activity / Initiation of Nuclear Envelope (NE) Reformation / Polo-like kinase mediated events / protein K11-linked ubiquitination / cyclin-dependent protein serine/threonine kinase activator activity / Golgi Cisternae Pericentriolar Stack Reorganization / enzyme-substrate adaptor activity / Condensation of Prometaphase Chromosomes / positive regulation of dendrite morphogenesis / regulation of mitotic metaphase/anaphase transition / cyclin-dependent protein serine/threonine kinase regulator activity / exit from mitosis / ubiquitin-ubiquitin ligase activity / mitotic metaphase chromosome alignment / E2 ubiquitin-conjugating enzyme / ubiquitin-like protein ligase binding / mitotic G2 DNA damage checkpoint signaling / negative regulation of cellular senescence / Regulation of APC/C activators between G1/S and early anaphase / ubiquitin conjugating enzyme activity / cullin family protein binding / protein K63-linked ubiquitination / Transcriptional Regulation by VENTX / ubiquitin-like ligase-substrate adaptor activity / positive regulation of axon extension / protein K48-linked ubiquitination / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / Regulation of MITF-M-dependent genes involved in cell cycle and proliferation / heterochromatin / Cyclin A/B1/B2 associated events during G2/M transition / Nuclear events stimulated by ALK signaling in cancer / Cyclin A:Cdk2-associated events at S phase entry / ubiquitin ligase complex / regulation of mitotic cell cycle / positive regulation of G2/M transition of mitotic cell cycle / Resolution of Sister Chromatid Cohesion / APC/C:Cdc20 mediated degradation of Cyclin B / APC-Cdc20 mediated degradation of Nek2A / positive regulation of mitotic cell cycle / nuclear periphery / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / mitotic spindle organization / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Condensation of Prophase Chromosomes / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / SCF-beta-TrCP mediated degradation of Emi1 / Assembly of the pre-replicative complex / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1 / brain development / protein modification process / mitotic spindle / CDK-mediated phosphorylation and removal of Cdc6 / kinetochore / spindle pole / spindle / protein polyubiquitination / ubiquitin-protein transferase activity
Similarity search - Function
: / Anaphase-promoting complex subunit 15 / The WD repeat Cdc20/Fizzy family / Anaphase-promoting complex subunit 15 / Anaphase-promoting complex subunit 4, metazoa / Anaphase-promoting complex subunit 1, C-terminal / Anaphase-promoting complex subunit 1, middle domain / : / : / : ...: / Anaphase-promoting complex subunit 15 / The WD repeat Cdc20/Fizzy family / Anaphase-promoting complex subunit 15 / Anaphase-promoting complex subunit 4, metazoa / Anaphase-promoting complex subunit 1, C-terminal / Anaphase-promoting complex subunit 1, middle domain / : / : / : / Anaphase-promoting complex subunit 1 WD40 beta-propeller domain / Anaphase-promoting complex sub unit 1 C-terminal domain / Anaphase-promoting complex subunit 1 middle domain / APC1 beta sandwich domain / Anaphase-promoting complex subunit 5, N-terminal domain / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex, subunit 16 / Cdc23 / Apc13 / Anaphase promoting complex subunit 8 / Cdc23 / Apc13p protein / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 4 long domain / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 5 domain / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex, cyclosome, subunit 4 / Anaphase-promoting complex subunit APC10/Doc1 / Anaphase-promoting complex, subunit CDC26 / Anaphase-promoting complex APC subunit CDC26 / Anaphase-promoting complex subunit 11, RING-H2 finger / Anaphase-promoting complex subunit 11 RING-H2 finger / Anaphase-promoting complex subunit 2, C-terminal / Anaphase-promoting complex subunit 2 / Anaphase promoting complex (APC) subunit 2 / Anaphase promoting complex (APC) subunit 2 / APC10/DOC domain / Anaphase-promoting complex, subunit 10 (APC10) / DOC domain profile. / Anaphase-promoting complex, subunit 10 (APC10) / Anaphase-promoting complex, cyclosome, subunit 3 / TPR repeat / : / Cyclin, C-terminal domain / : / Cyclins signature. / Cyclin / Tetratricopeptide repeat / Cyclin, C-terminal domain / Cyclin_C / Anaphase-promoting complex subunit 4, WD40 domain / : / : / Anaphase-promoting complex subunit 4 WD40 domain / Cullin / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin family / Cullin family profile. / Tetratricopeptide repeat / Tetratricopeptide repeat / Cyclin, N-terminal / Cyclin, N-terminal domain / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Tetratricopeptide repeat / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Ubiquitin-conjugating enzyme/RWD-like / Cyclin-like superfamily / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Galactose-binding-like domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / Armadillo-like helical / Tetratricopeptide-like helical domain superfamily / Zinc finger, RING/FYVE/PHD-type / Winged helix DNA-binding domain superfamily / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / Winged helix-like DNA-binding domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 C / G2/mitotic-specific cyclin-B1 / Cell division cycle protein 27 homolog / Anaphase-promoting complex subunit 15 / Cell division cycle protein 16 homolog / Ubiquitin-conjugating enzyme E2 S / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 ...Ubiquitin-conjugating enzyme E2 C / G2/mitotic-specific cyclin-B1 / Cell division cycle protein 27 homolog / Anaphase-promoting complex subunit 15 / Cell division cycle protein 16 homolog / Ubiquitin-conjugating enzyme E2 S / Anaphase-promoting complex subunit CDC26 / Anaphase-promoting complex subunit 16 / Anaphase-promoting complex subunit 13 / Anaphase-promoting complex subunit 1 / Anaphase-promoting complex subunit 11 / Cell division cycle protein 23 homolog / Anaphase-promoting complex subunit 7 / Anaphase-promoting complex subunit 5 / Anaphase-promoting complex subunit 4 / Anaphase-promoting complex subunit 2 / Fizzy-related protein homolog / Anaphase-promoting complex subunit 10
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsBodrug T / Welsh KA / Bolhuis DL / Paulakonis E / Martinez-Chacin RC / Liu B / Pinkin N / Bonacci T / Cui L / Xu P ...Bodrug T / Welsh KA / Bolhuis DL / Paulakonis E / Martinez-Chacin RC / Liu B / Pinkin N / Bonacci T / Cui L / Xu P / Roscow O / Amann SJ / Grishkovskaya I / Emanuele MJ / Harrison JS / Steimel JP / Hahn KM / Zhang W / Zhong E / Haselbach D / Brown NG
Funding support United States, Austria, 4 items
OrganizationGrant numberCountry
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)T32GM008570 United States
Vienna Science and Technology Fund (WWTF)WWTF-LS19-029 Austria
National Institutes of Health/Eunice Kennedy Shriver National Institute of Child Health & Human Development (NIH/NICHD)R35GM128855 United States
National Science Foundation (NSF, United States)DGE-1650116 United States
CitationJournal: Nat Struct Mol Biol / Year: 2023
Title: Time-resolved cryo-EM (TR-EM) analysis of substrate polyubiquitination by the RING E3 anaphase-promoting complex/cyclosome (APC/C).
Authors: Tatyana Bodrug / Kaeli A Welsh / Derek L Bolhuis / Ethan Paulаkonis / Raquel C Martinez-Chacin / Bei Liu / Nicholas Pinkin / Thomas Bonacci / Liying Cui / Pengning Xu / Olivia Roscow / ...Authors: Tatyana Bodrug / Kaeli A Welsh / Derek L Bolhuis / Ethan Paulаkonis / Raquel C Martinez-Chacin / Bei Liu / Nicholas Pinkin / Thomas Bonacci / Liying Cui / Pengning Xu / Olivia Roscow / Sascha Josef Amann / Irina Grishkovskaya / Michael J Emanuele / Joseph S Harrison / Joshua P Steimel / Klaus M Hahn / Wei Zhang / Ellen D Zhong / David Haselbach / Nicholas G Brown /
Abstract: Substrate polyubiquitination drives a myriad of cellular processes, including the cell cycle, apoptosis and immune responses. Polyubiquitination is highly dynamic, and obtaining mechanistic insight ...Substrate polyubiquitination drives a myriad of cellular processes, including the cell cycle, apoptosis and immune responses. Polyubiquitination is highly dynamic, and obtaining mechanistic insight has thus far required artificially trapped structures to stabilize specific steps along the enzymatic process. So far, how any ubiquitin ligase builds a proteasomal degradation signal, which is canonically regarded as four or more ubiquitins, remains unclear. Here we present time-resolved cryogenic electron microscopy studies of the 1.2 MDa E3 ubiquitin ligase, known as the anaphase-promoting complex/cyclosome (APC/C), and its E2 co-enzymes (UBE2C/UBCH10 and UBE2S) during substrate polyubiquitination. Using cryoDRGN (Deep Reconstructing Generative Networks), a neural network-based approach, we reconstruct the conformational changes undergone by the human APC/C during polyubiquitination, directly visualize an active E3-E2 pair modifying its substrate, and identify unexpected interactions between multiple ubiquitins with parts of the APC/C machinery, including its coactivator CDH1. Together, we demonstrate how modification of substrates with nascent ubiquitin chains helps to potentiate processive substrate polyubiquitination, allowing us to model how a ubiquitin ligase builds a proteasomal degradation signal.
History
DepositionJun 27, 2023-
Header (metadata) releaseSep 27, 2023-
Map releaseSep 27, 2023-
UpdateDec 13, 2023-
Current statusDec 13, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_41142.png

Downloads & links

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Map

FileDownload / File: emd_41142.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.1 Å/pix.
x 400 pix.
= 440. Å		1.1 Å/pix.
x 400 pix.
= 440. Å		1.1 Å/pix.
x 400 pix.
= 440. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.025
Minimum - Maximum-0.0396715 - 1.8597358
Average (Standard dev.)0.0015470746 (±0.0271046)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 440.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_41142_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_41142_half_map_2.map
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Sample components

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Entire : Anaphase-Promoting Complex/Cyclosome in complex with CDH1, UBE2C,...

EntireName: Anaphase-Promoting Complex/Cyclosome in complex with CDH1, UBE2C, UBE2S, Cyclin-B
Components
  • Complex: Anaphase-Promoting Complex/Cyclosome in complex with CDH1, UBE2C, UBE2S, Cyclin-B
    • Protein or peptide: Anaphase-promoting complex subunit 1
    • Protein or peptide: G2/mitotic-specific cyclin-B1
    • Protein or peptide: Anaphase-promoting complex subunit 11
    • Protein or peptide: Anaphase-promoting complex subunit 15
    • Protein or peptide: Ubiquitin-conjugating enzyme E2 S
    • Protein or peptide: Anaphase-promoting complex subunit CDC26
    • Protein or peptide: Anaphase-promoting complex subunit 16
    • Protein or peptide: Anaphase-promoting complex subunit 4
    • Protein or peptide: Cell division cycle protein 27 homolog
    • Protein or peptide: Cell division cycle protein 16 homolog
    • Protein or peptide: Anaphase-promoting complex subunit 10
    • Protein or peptide: Anaphase-promoting complex subunit 13
    • Protein or peptide: Anaphase-promoting complex subunit 2
    • Protein or peptide: Anaphase-promoting complex subunit 5
    • Protein or peptide: Ubiquitin-conjugating enzyme E2 C
    • Protein or peptide: Fizzy-related protein homolog
    • Protein or peptide: Cell division cycle protein 23 homolog
    • Protein or peptide: Anaphase-promoting complex subunit 7
  • Ligand: ZINC ION

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Supramolecule #1: Anaphase-Promoting Complex/Cyclosome in complex with CDH1, UBE2C,...

SupramoleculeName: Anaphase-Promoting Complex/Cyclosome in complex with CDH1, UBE2C, UBE2S, Cyclin-B
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18
Molecular weightTheoretical: 1.16 MDa

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Macromolecule #1: Anaphase-promoting complex subunit 1

MacromoleculeName: Anaphase-promoting complex subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 217.566141 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGEDVDY DEELYVAGNM VIWSKGSKSQ ALAVYKAFTV DSPVQQALWC DFIISQDKSE KAYSSNEVEK CICILQSSCI N MHSIEGKD ...String:
MSNFYEERTT MIAARDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS LQEVTIHEKQ KESWQLRKGV SEIGEDVDY DEELYVAGNM VIWSKGSKSQ ALAVYKAFTV DSPVQQALWC DFIISQDKSE KAYSSNEVEK CICILQSSCI N MHSIEGKD YIASLPFQVA NVWPTKYGLL FERSASSHEV PPGEPREPLP TMFSMLHPLD EITPLVCKSG SLFGSSRVQY VV DHAMKIV FLNTDPSIVM TYDAVQNVHS VWTLRRVKSE EENVVLKFEE QGGEPQNVAT SSSLTAHLRS LSKGDEPVEE PFQ NYSSIH SQSRSTSEPS LHSREPEISN MAALSRAHEP ALGVHEFSGV QRFNIESHNQ EPKRHSISHS PNSNSNGSFL APET EPIVP ELCIDHLWTE TITNIREKNS QASKVFITSD LCGQKFLCFL VESQLQLRCV KFQESNDKTQ LIFGSVTNIP AKDAA PVEK IDTMLVLEGS GNLVLYTGVV RVGKVFIPGL PAPSLTMSNT MPRPSTPLDG VSEPKPLSKL LGELDEVVLL EPVPEL RDS SKLHDELYNE DCTFQQLGTY IHSIRDPVHN RVTLELSNGS MVRITIPEIA TSELVQTCLQ AIKFILPKEI AVQMLVK WY NVHSAPGGPS YHSEWNLFVT CLMNMMGYNT DRLAWTRNFD FEGSLEPVIA PKKARPEETG SDDDWEYLLN SDYHQNVE S HLLNRSLCLS PSEASQMKDE DFSQNLSLDS STLLFTHIPA IFFVLHLVYE ELKLNTLMGE GICSLVELLV QLARDLKLG PYVDHYYRDY PTLVRTTGQV CTIDPGQTGF MHHPSFFTSE PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY ILGDESLVS DESSQYLTRI TIAPQKLQVE QEENRFEFRH STSVSSLAER LVVWMTNVGF TLRDLETLPF GIALPIRDAI Y HCREQPAS DWPEAVCLLI GRQDLSKQAC EGNLPKGKSV LSSDVPSGTE TEEEDDGMND MNHEVMSLIW SEDLRVQDVR RL LQSAHPV RVNVVQYPEL SDHEFIEEKE NRLLQLCQRT MALPVGRGMF TLFSYHPVPT EPLPIPKLNL TGRAPPRNTT VDL NSGNID VPPNMTSWAS FHNGVAAGLK IAPASQIDSA WIVYNKPKHA ELANEYAGFL MALGLNGHLT KLATLNIHDY LTKG HEMTS IGLLLGVSAA KLGTMDMSIT RLLSIHIPAL LPPTSTELDV PHNVQVAAVV GIGLVYQGTA HRHTAEVLLA EIGRP PGPE MEYCTDRESY SLAAGLALGM VCLGHGSNLI GMSDLNVPEQ LYQYMVGGHR RFQTGMHREK HKEPSYQIKE GDTINV DVT CPGATLALAM IYLKTNNRSI ADWLRAPDTM YLLDFVKPEF LLLRTLARCL ILWDDILPNS KWVDSNVPQI IRENSIS LS EIELPCSEDL NLETLSQAHV YIIAGACLSL GFRFAGSENL SAFNCLHKFA KDFMTYLSAP NASVTGPHNL ETCLSVVL L SLAMVMAGSG NLKVLQLCRF LHMKTGGEMN YGFHLAHHMA LGLLFLGGGR YSLSTSNSSI AALLCALYPH FPAHSTDNR YHLQALRHLY VLAAEPRLLV PVDVDTNTPC YALLEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQIKVKG PRYWELLIDL SKGTQHLKS ILSKDGVLYV KLRAGQLSYK EDPMGWQSLL AQTVANRNSE ARAFKPETIS AFTSDPALLS FAEYFCKPTV N MGQKQEIL DLFSSVLYEC VTQETPEMLP AYIAMDQAIR RLGRREMSET SELWQIKLVL EFFSSRSHQE RLQNHPKRGL FM NSEFLPV VKCTIDNTLD QWLQVGGDMC VHAYLSGQPL EESQLSMLAC FLVYHSVPAP QHLPPIGLEG STSFAELLFK FKQ LKMPVR ALLRLAPLLL GNPQPMVM

UniProtKB: Anaphase-promoting complex subunit 1

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Macromolecule #2: G2/mitotic-specific cyclin-B1

MacromoleculeName: G2/mitotic-specific cyclin-B1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.284467 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
LRPRTALGDI GN

UniProtKB: G2/mitotic-specific cyclin-B1

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Macromolecule #3: Anaphase-promoting complex subunit 11

MacromoleculeName: Anaphase-promoting complex subunit 11 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.854647 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MKVKIKCWNG VATWLWVAND ENCGICRMAF NGCCPDCKVP GDDCPLVWGQ CSHCFHMHCI LKWLHAQQVQ QHCPMCRQEW KFKE

UniProtKB: Anaphase-promoting complex subunit 11

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Macromolecule #4: Anaphase-promoting complex subunit 15

MacromoleculeName: Anaphase-promoting complex subunit 15 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 6.556302 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
STLFPSLFPR VTETLWFNLD RPCVEETELQ QQEQQHQAWL QSIAEKDNNL VPIGKP

UniProtKB: Anaphase-promoting complex subunit 15

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Macromolecule #5: Ubiquitin-conjugating enzyme E2 S

MacromoleculeName: Ubiquitin-conjugating enzyme E2 S / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: E2 ubiquitin-conjugating enzyme
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 2.162754 KDa
SequenceString:
KKLAAKKKTD KKRALRRL

UniProtKB: Ubiquitin-conjugating enzyme E2 S

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Macromolecule #6: Anaphase-promoting complex subunit CDC26

MacromoleculeName: Anaphase-promoting complex subunit CDC26 / type: protein_or_peptide / ID: 6 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.920108 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL EEDPKSREQM INDRIGYKPQ PKPNNRSSQF GELEF

UniProtKB: Anaphase-promoting complex subunit CDC26

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Macromolecule #7: Anaphase-promoting complex subunit 16

MacromoleculeName: Anaphase-promoting complex subunit 16 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.677995 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MAASSSSSSA GGVSGSSVTG SGFSVSDLAP PRKALFTYPK GAGEMLEDGS ERFLCESVFS YQVASTLKQV KHDQQVARME KLAGLVEEL EADEWRFKPI EQLLGFTPSS G

UniProtKB: Anaphase-promoting complex subunit 16

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Macromolecule #8: Anaphase-promoting complex subunit 4

MacromoleculeName: Anaphase-promoting complex subunit 4 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 92.303305 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKK IVLCDVEKPE SLHSFSVEAP VSCMHWMEVT VESSVLTSFY NAEDESNLLL PKLPTLPKNY SNTSKIFSEE N SDEIIKLL ...String:
MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKK IVLCDVEKPE SLHSFSVEAP VSCMHWMEVT VESSVLTSFY NAEDESNLLL PKLPTLPKNY SNTSKIFSEE N SDEIIKLL GDVRLNILVL GGSSGFIELY AYGMFKIARV TGIAGTCLAL CLSSDLKSLS VVTEVSTNGA SEVSYFQLET NL LYSFLPE VTRMARKFTH ISALLQYINL SLTCMCEAWE EILMQMDSRL TKFVQEKNTT TSVQDEFMHL LLWGKASAEL QTL LMNQLT VKGLKKLGQS IESSYSSIQK LVISHLQSGS ESLLYHLSEL KGMASWKQKY EPLGLDAAGI EEAITAVGSF ILKA NELLQ VIDSSMKNFK AFFRWLYVAM LRMTEDHVLP ELNKMTQKDI TFVAEFLTEH FNEAPDLYNR KGKYFNVERV GQYLK DEDD DLVSPPNTEG NQWYDFLQNS SHLKESPLLF PYYPRKSLHF VKRRMENIID QCLQKPADVI GKSMNQAICI PLYRDT RSE DSTRRLFKFP FLWNNKTSNL HYLLFTILED SLYKMCILRR HTDISQSVSN GLIAIKFGSF TYATTEKVRR SIYSCLD AQ FYDDETVTVV LKDTVGREGR DRLLVQLPLS LVYNSEDSAE YQFTGTYSTR LDEQCSAIPT RTMHFEKHWR LLESMKAQ Y VAGNGFRKVS CVLSSNLRHV RVFEMDIDDE WELDESSDEE EEASNKPVKI KEEVLEEEEA ENQQAGAAAL APEIVIKVE KLDPELDS

UniProtKB: Anaphase-promoting complex subunit 4

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Macromolecule #9: Cell division cycle protein 27 homolog

MacromoleculeName: Cell division cycle protein 27 homolog / type: protein_or_peptide / ID: 9 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 92.519547 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGE QILSGGVFNK QKSHDDIVTE FGDSACFTLS LLGHVYCKTD RLAKGSECYQ KSLSLNPFLW SPFESLCEIG E KPDPDQTF ...String:
MTVLQEPVQA AIWQALNHYA YRDAVFLAER LYAEVHSEEA LFLLATCYYR SGKAYKAYRL LKGHSCTTPQ CKYLLAKCCV DLSKLAEGE QILSGGVFNK QKSHDDIVTE FGDSACFTLS LLGHVYCKTD RLAKGSECYQ KSLSLNPFLW SPFESLCEIG E KPDPDQTF KFTSLQNFSN CLPNSCTTQV PNHSLSHRQP EEVLTEEPQD TIELNRLNLE SENSKYSLNT DSSVSYIDSA VI EPDTVPL GTGTSILSKQ VQNKPKTGRS LLGGPAALEP LTPSFGILPL ETPSPGDGSY LQNYTNTPPV IDVPSTGAPS KKE VARIGQ TGTKSVFSQE GNEREVTPIL AQTQSSGPQT STTPQVLSPT ITSPPNALPR RSSRLFTSDE ETTKENEKKL KMKF PPKIP NRKTKSKTNK GGITQPNIND ELEITKLDSE IISEGKISTI EPQIQAFNLQ KAAAEGLMSL LREMGKGYLA LCSYN CKEA INILSHLPSH HYNTGWVLCQ IGRAYFELSE YMQAERIFSE VRRIENYRVE GMEIYSTTLW HLQKDVALSV LSKDLT DMD KNSPEAWCAA GNCFSLQREH DIAIKFFQRA IQVDPNYAYA YTLLGHEFVL TEELDKALAC FRNAIRVNPR HYNAWYG LG MIYYKQEKFS LAEMHFQKAL DINPQSSVLL CHIGVVQHAL KKSEKALDTL NKAIVIDPKN PLCKFHRASV LFANEKYK S ALQELEELKQ IVPKESLVYF LIGKVYKKLG QTHLALMNFS WAMDLDPKGA NNQIKEAIDK RYLPDDEEPI TQEEQIMGT DESQESSMTD ADDTQLHAAE SDEF

UniProtKB: Cell division cycle protein 27 homolog

+
Macromolecule #10: Cell division cycle protein 16 homolog

MacromoleculeName: Cell division cycle protein 16 homolog / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 71.929656 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQA LDVLDMEEPI NKRLFEKYLK DEEGFKDPSS DWEMSQSSIK SSICLLRGKI YDALDNRTLA TYSYKEALKL D VYCFEAFD ...String:
MNLERLRKRV RQYLDQQQYQ SALFWADKVA SLSREEPQDI YWLAQCLYLT AQYHRAAHAL RSRKLDKLYE ACRYLAARCH YAAKEHQQA LDVLDMEEPI NKRLFEKYLK DEEGFKDPSS DWEMSQSSIK SSICLLRGKI YDALDNRTLA TYSYKEALKL D VYCFEAFD LLTSHHMLTA QEEKELLESL PLSKLCNEEQ ELLRFLFENK LKKYNKPSET VIPESVDGLQ ENLDVVVSLA ER HYYNCDF KMCYKLTSVV MEKDPFHASC LPVHIGTLVE LNKANELFYL SHKLVDLYPS NPVSWFAVGC YYLMVGHKNE HAR RYLSKA TTLEKTYGPA WIAYGHSFAV ESEHDQAMAA YFTAAQLMKG CHLPMLYIGL EYGLTNNSKL AERFFSQALS IAPE DPFVM HEVGVVAFQN GEWKTAEKWF LDALEKIKAI GNEVTVDKWE PLLNNLGHVC RKLKKYAEAL DYHRQALVLI PQNAS TYSA IGYIHSLMGN FENAVDYFHT ALGLRRDDTF SVTMLGHCIE MYIGDSEAYI GADIKDKLKC YDFDVHTMKT LKNIIE PPW DFREFEVEKQ TAEETGLEPL EEERKTPDSR PSLEETFEIE MNESDMMLET SMSDHST

UniProtKB: Cell division cycle protein 16 homolog

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Macromolecule #11: Anaphase-promoting complex subunit 10

MacromoleculeName: Anaphase-promoting complex subunit 10 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.310152 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MTEPNKTPPG ADPKQLERTG TVREIGSQAV WSLSSCKPGF GVDQLRDDNL ETYWQSDGSQ PHLVNIQFRR KTTVKTLCIY ADYKSDESY TPSKISVRVG NNFHNLQEIR QLELVEPSGW IHVPLTDNHK KPTRTFMIQI AVLANHQNGR DTHMRQIKIY T PVEESSIG KFPRCTTIDF MMYRSIR

UniProtKB: Anaphase-promoting complex subunit 10

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Macromolecule #12: Anaphase-promoting complex subunit 13

MacromoleculeName: Anaphase-promoting complex subunit 13 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.528309 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MDSEVQRDGR ILDLIDDAWR EDKLPYEDVA IPLNELPEPE QDNGGTTESV KEQEMKWTDL ALQYLHENVP PIGN

UniProtKB: Anaphase-promoting complex subunit 13

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Macromolecule #13: Anaphase-promoting complex subunit 2

MacromoleculeName: Anaphase-promoting complex subunit 2 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 94.149156 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISP EFWNAISQCE NSADEPQCLL LLLDAFGLLE SRLDPYLRSL ELLEKWTRLG LLMGTGAQGL REEVHTMLRG V LFFSTPRT ...String:
MAAAVVVAEG DSDSRPGQEL LVAWNTVSTG LVPPAALGLV SSRTSGAVPP KEEELRAAVE VLRGHGLHSV LEEWFVEVLQ NDLQANISP EFWNAISQCE NSADEPQCLL LLLDAFGLLE SRLDPYLRSL ELLEKWTRLG LLMGTGAQGL REEVHTMLRG V LFFSTPRT FQEMIQRLYG CFLRVYMQSK RKGEGGTDPE LEGELDSRYA RRRYYRLLQE PLCAGCSSDK QQCWCRQALE QF HQLSQVL HRLSLLERVS AEAVTTTLHQ VTRERMEDRC RGEYERSFLR EFHKWIERVV GWLGKVFLQD GPARPAEPEA GNT LRRWRC HVQRFFYRIY ASLRIEELFS IVRDFPDSRP AIEDLKYCLE RTDQRQQLLV SLKAALETRL LHPGVNTCDI ITLY ISAIK ALRVLDPSMV ILEVACEPIR RYLRTREDTV RQIVAGLTGD SDGTGDLAVE LSKTDPASLE TGQDEEDDSG EPEDW VPDP VDADPGKSSS KRRSSDIISL LVSIYGSKDL FINEYRSLLA DRLLHQFSFE PEREIRNVEL LKLRFGEAPM HFCEVM LKD MADSRRINAN IREEDEKRPA EEQPPFGVYA VILSSEFWPP FKDEKLEVPE DIRAALEAYC KKYEQLKAMR TLSWKHT LG LVTMDVELAD RTLSVAVTPV QAVILLYFQD QASWTLEELS KAVKMPVALL RRRMSVWLQQ GVLREEPPGT FSVIEEER P QDRDNMVLID SDDESDSGMA SQADQKEEEL LLFWTYIQAM LTNLESLSLD RIYNMLRMFV VTGPALAEID LQELQGYLQ KKVRDQQLVY EAGVYRLPKN CS

UniProtKB: Anaphase-promoting complex subunit 2

+
Macromolecule #14: Anaphase-promoting complex subunit 5

MacromoleculeName: Anaphase-promoting complex subunit 5 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 85.445961 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL NQLLLPLLQG PDITLSKLYK LIEESCPQL ANSVQIRIKL MAEGELKDME QFFDDLSDSF SGTEPEVHKT SVVGLFLRHM ILAYSKLSFS QVFKLYTALQ Q YFQNGEKK ...String:
MASVHESLYF NPMMTNGVVH ANVFGIKDWV TPYKIAVLVL LNEMSRTGEG AVSLMERRRL NQLLLPLLQG PDITLSKLYK LIEESCPQL ANSVQIRIKL MAEGELKDME QFFDDLSDSF SGTEPEVHKT SVVGLFLRHM ILAYSKLSFS QVFKLYTALQ Q YFQNGEKK TVEDADMELE ERDEGERKME KEELDVEVRE EEVECSGPLS QKQAEFFLSQ QAELLKNDET KALEPASLQK EL NNLLKFN PDFAEAHYLS YLNNLRVQDV FSSTHSLLHY FDRLILTGAE SKSNGEEGYG RSLRYAALNL AALHCRFGHY QQA ELALQE AIRIAQESND HVCLQHCLSW LYVLGQKRSD SYVLLEHEVK KAVHFGLPYL ASLGIQSLVQ QRAFAGKTAN KLMD ALKDS DLLHWKHSLS ELIDISIAQK TAIWRLYGRS TMALQQAQML LSMNSLEAVN AGVQQNNTES FAVALCHLAE LHAEQ GCFA AASEVLKHLK ERFPPNSQHA QLWMLCDQKI QFDRAMNDGK YHLADSLVTG ITALNSIEGV YRKAVVLQAQ NQMSEA HKL LQKLLVHCQK LKNTEMVISV LLSVAELYWR SSSPTIALPM LLQALALSKE YRLQYLASET VLNLAFAQLI LGIPEQA LS LLHMAIEPIL ADGAILDKGR AMFLVAKCQV ASAASYDQPK KAEALEAAIE NLNEAKNYFA KVDCKERIRD VVYFQARL Y HTLGKTQERN RCAMLFRQLH QELPSHGVPL INHL

UniProtKB: Anaphase-promoting complex subunit 5

+
Macromolecule #15: Ubiquitin-conjugating enzyme E2 C

MacromoleculeName: Ubiquitin-conjugating enzyme E2 C / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO / EC number: E2 ubiquitin-conjugating enzyme
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 19.673262 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MASQNRDPAA TSVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI SAFPESDNLF KWVGTIHGAA GTVYEDLRYK LSLEFPSGY PYNAPTVKFL TPCYHPNVDT QGNICLDILK EKWSALYDVR TILLSIQSLL GEPNIDSPLN THAAELWKNP T AFKKYLQE TYSKQVTSQE P

UniProtKB: Ubiquitin-conjugating enzyme E2 C

+
Macromolecule #16: Fizzy-related protein homolog

MacromoleculeName: Fizzy-related protein homolog / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.253207 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP SRAGANWSVN FHRINENEKS PSQNRKAKDA TSDNGKDGL AYSALLKNEL LGAGIEKVQD PQTEDRRLQP STPEKKGLFT YSLSTKRSSP DDGNDVSPYS LSPVSNKSQK L LRSPRKPT ...String:
MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP SRAGANWSVN FHRINENEKS PSQNRKAKDA TSDNGKDGL AYSALLKNEL LGAGIEKVQD PQTEDRRLQP STPEKKGLFT YSLSTKRSSP DDGNDVSPYS LSPVSNKSQK L LRSPRKPT RKISKIPFKV LDAPELQDDF YLNLVDWSSL NVLSVGLGTC VYLWSACTSQ VTRLCDLSVE GDSVTSVGWS ER GNLVAVG THKGFVQIWD AAAGKKLSML EGHTARVGAL AWNAEQLSSG SRDRMILQRD IRTPPLQSER RLQGHRQEVC GLK WSTDHQ LLASGGNDNK LLVWNHSSLS PVQQYTEHLA AVKAIAWSPH QHGLLASGGG TADRCIRFWN TLTGQPLQCI DTGS QVCNL AWSKHANELV STHGYSQNQI LVWKYPSLTQ VAKLTGHSYR VLYLAMSPDG EAIVTGAGDE TLRFWNVFSK TRSTK VKWE SVSVLNLFTR IR

UniProtKB: Fizzy-related protein homolog

+
Macromolecule #17: Cell division cycle protein 23 homolog

MacromoleculeName: Cell division cycle protein 23 homolog / type: protein_or_peptide / ID: 17 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 69.075133 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTL AKAYFDVKEY DRAAHFLHGC NSKKAYFLYM YSRYLSGEKK KDDETVDSLG PLEKGQVKNE ALRELRVELS K KHQARELD ...String:
MAASTSMVPV AVTAAVAPVL SINSDFSDLR EIKKQLLLIA GLTRERGLLH SSKWSAELAF SLPALPLAEL QPPPPITEED AQDMDAYTL AKAYFDVKEY DRAAHFLHGC NSKKAYFLYM YSRYLSGEKK KDDETVDSLG PLEKGQVKNE ALRELRVELS K KHQARELD GFGLYLYGVV LRKLDLVKEA IDVFVEATHV LPLHWGAWLE LCNLITDKEM LKFLSLPDTW MKEFFLAHIY TE LQLIEEA LQKYQNLIDV GFSKSSYIVS QIAVAYHNIR DIDKALSIFN ELRKQDPYRI ENMDTFSNLL YVRSMKSELS YLA HNLCEI DKYRVETCCV IGNYYSLRSQ HEKAALYFQR ALKLNPRYLG AWTLMGHEYM EMKNTSAAIQ AYRHAIEVNK RDYR AWYGL GQTYEILKMP FYCLYYYRRA HQLRPNDSRM LVALGECYEK LNQLVEAKKC YWRAYAVGDV EKMALVKLAK LHEQL TESE QAAQCYIKYI QDIYSCGEIV EHLEESTAFR YLAQYYFKCK LWDEASTCAQ KCCAFNDERE EGKALLRQIL QLRNQG EEP TTEVPAPFFL PASLSANNEP TRRVEPLNLS SVEP

UniProtKB: Cell division cycle protein 23 homolog

+
Macromolecule #18: Anaphase-promoting complex subunit 7

MacromoleculeName: Anaphase-promoting complex subunit 7 / type: protein_or_peptide / ID: 18 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 63.20402 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MNVIDHVRDM AAAGLHSNVR LLSSLLLTMS NNNPELFSPP QKYQLLVYHA DSLFHDKEYR NAVSKYTMAL QQKKALSKTS KVRPSTGNS ASTPQSQCLP SEIEVKYKMA ECYTMLKQDK DAIAILDGIP SRQRTPKINM MLANLYKKAG QERPSVTSYK E VLRQCPLA ...String:
MNVIDHVRDM AAAGLHSNVR LLSSLLLTMS NNNPELFSPP QKYQLLVYHA DSLFHDKEYR NAVSKYTMAL QQKKALSKTS KVRPSTGNS ASTPQSQCLP SEIEVKYKMA ECYTMLKQDK DAIAILDGIP SRQRTPKINM MLANLYKKAG QERPSVTSYK E VLRQCPLA LDAILGLLSL SVKGAEVASM TMNVIQTVPN LDWLSVWIKA YAFVHTGDNS RAISTICSLE KKSLLRDNVD LL GSLADLY FRAGDNKNSV LKFEQAQMLD PYLIKGMDVY GYLLAREGRL EDVENLGCRL FNISDQHAEP WVVSGCHSFY SKR YSRALY LGAKAIQLNS NSVQALLLKG AALRNMGRVQ EAIIHFREAI RLAPCRLDCY EGLIECYLAS NSIREAMVMA NNVY KTLGA NAQTLTLLAT VCLEDPVTQE KAKTLLDKAL TQRPDYIKAV VKKAELLSRE QKYEDGIALL RNALANQSDC VLHRI LGDF LVAVNEYQEA MDQYSIALSL DPNDQKSLEG MQKMEKEESP TDATQEEDVD DMEGSGEEGD LEGSDSEAAQ WADQEQ WFG MQ

UniProtKB: Anaphase-promoting complex subunit 7

+
Macromolecule #19: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 19 / Number of copies: 4 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 BASE (4k x 4k) / Average electron dose: 42.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 774933
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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