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- EMDB-56717: Human PRC1.4 bound to a H3Kc27me3 mononucleosome -

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Basic information

Entry
Database: EMDB / ID: EMD-56717
TitleHuman PRC1.4 bound to a H3Kc27me3 mononucleosome
Map dataMain Map
Sample
  • Complex: Human PRC1.4 bound to a H3Kc27me3 mononucleosome
    • Protein or peptide: x 12 types
    • DNA: x 2 types
KeywordsPRC1 / nucleosome / GENE REGULATION / H3Kc27me3
Function / homology
Function and homology information


histone H2AK119 ubiquitin ligase activity / segment specification / RING-like zinc finger domain binding / ubiquitin-protein transferase activator activity / positive regulation of immature T cell proliferation in thymus / sex chromatin / germ cell development / PcG protein complex / PRC1 complex / SUMOylation of DNA methylation proteins ...histone H2AK119 ubiquitin ligase activity / segment specification / RING-like zinc finger domain binding / ubiquitin-protein transferase activator activity / positive regulation of immature T cell proliferation in thymus / sex chromatin / germ cell development / PcG protein complex / PRC1 complex / SUMOylation of DNA methylation proteins / SUMOylation of RNA binding proteins / positive regulation of ubiquitin-protein transferase activity / negative regulation of gene expression, epigenetic / hemopoiesis / Transcriptional Regulation by E2F6 / Differentiation of naive CD4+ T cells to T helper 2 cells (Th2 cells) / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / MLL1 complex / positive regulation of B cell proliferation / SUMOylation of DNA damage response and repair proteins / ubiquitin ligase complex / heterochromatin / SUMOylation of transcription cofactors / positive regulation of fibroblast proliferation / Regulation of PTEN gene transcription / SUMOylation of chromatin organization proteins / promoter-specific chromatin binding / epigenetic regulation of gene expression / euchromatin / RING-type E3 ubiquitin transferase / regulation of gene expression / ubiquitin protein ligase activity / heterochromatin formation / Oxidative Stress Induced Senescence / nuclear body / protein ubiquitination / chromosome / chromatin remodeling / ribonucleoprotein complex / negative regulation of DNA-templated transcription / chromatin binding / positive regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / nucleoplasm / zinc ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Chromobox protein homolog 7 / CBX family C-terminal motif / CBX family C-terminal motif / E3 ubiquitin-protein ligase RING2 / E3 ubiquitin-protein ligase RING1/RING2 / RAWUL domain / RAWUL domain RING finger- and WD40-associated ubiquitin-like / Chromo domain subgroup / Zinc finger, C3HC4 type (RING finger) / Chromo domain, conserved site ...Chromobox protein homolog 7 / CBX family C-terminal motif / CBX family C-terminal motif / E3 ubiquitin-protein ligase RING2 / E3 ubiquitin-protein ligase RING1/RING2 / RAWUL domain / RAWUL domain RING finger- and WD40-associated ubiquitin-like / Chromo domain subgroup / Zinc finger, C3HC4 type (RING finger) / Chromo domain, conserved site / Chromo domain signature. / Chromo domain / Chromo (CHRromatin Organisation MOdifier) domain / Chromo and chromo shadow domain profile. / Chromo/chromo shadow domain / Chromatin organization modifier domain / Chromo-like domain superfamily / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type
Similarity search - Domain/homology
Chromobox 7 / Polycomb complex protein BMI-1 / Isoform 2 of Polyhomeotic-like protein 2 / E3 ubiquitin-protein ligase RING2
Similarity search - Component
Biological speciesHomo sapiens (human) / Xenopus (frog)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.72 Å
AuthorsCiapponi M / Mueller J
Funding support Germany, 1 items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
CitationJournal: Nat Struct Mol Biol / Year: 2026
Title: Cryo-EM structure, enzymatic activity and genome targeting of canonical PRC1.
Authors: Maria Ciapponi / Martina Cafiso / Sven Schkölziger / Christian Benda / Jacques Bonnet / Jürg Müller /
Abstract: Canonical Polycomb repressive complex 1 (cPRC1) preserves cell fate decisions by repressing aberrant transcription of developmental regulator genes. We report the cryo-electron microscopy structure ...Canonical Polycomb repressive complex 1 (cPRC1) preserves cell fate decisions by repressing aberrant transcription of developmental regulator genes. We report the cryo-electron microscopy structure of the human cPRC1 holocomplex assembled from RING1B, BMI1, PHC2 and CBX7 bound to an H3K27me3-modified mononucleosome together with the ubiquitin-conjugating enzyme UBCH5C. cPRC1 adopts a compact, highly integrated architecture in which the subunits RING1B, BMI1 and PHC2 form an extended interface that positions UBCH5C on the nucleosome to enable efficient monoubiquitination of histone H2A at K119. This organization is conserved in Drosophila, where mutational analyses identify the PHC2 ortholog Polyhomeotic (Ph) as a central scaffold and targeting factor. The Ph HD domain is required for complex assembly, whereas the Ph SAM domain is dispensable for assembly but essential for cPRC1 recruitment to Polycomb target genes and productive H2A monoubiquitination at these loci.
History
DepositionFeb 12, 2026-
Header (metadata) releaseSep 16, 2026-
Map releaseSep 16, 2026-
UpdateSep 23, 2026-
Current statusSep 23, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_56717.png

Downloads & links

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Map

FileDownload / File: emd_56717.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMain Map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 400 pix.
= 340.48 Å		0.85 Å/pix.
x 400 pix.
= 340.48 Å		0.85 Å/pix.
x 400 pix.
= 340.48 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.8512 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.08
Minimum - Maximum-0.13357385 - 0.35503182
Average (Standard dev.)0.00012765576 (±0.012921604)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 340.47998 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_56717_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map A

Fileemd_56717_half_map_1.map
AnnotationHalf map A
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Half map B

Fileemd_56717_half_map_2.map
AnnotationHalf map B
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Human PRC1.4 bound to a H3Kc27me3 mononucleosome

EntireName: Human PRC1.4 bound to a H3Kc27me3 mononucleosome
Components
  • Complex: Human PRC1.4 bound to a H3Kc27me3 mononucleosome
    • Protein or peptide: Polyhomeotic-like protein 2, isoform B
    • Protein or peptide: Chromobox 7
    • Protein or peptide: E3 ubiquitin-protein ligase RING2
    • Protein or peptide: Polycomb complex protein BMI-1
    • Protein or peptide: Histone H3Kc27me3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • DNA: DNA (151-MER)
    • DNA: DNA (151-MER)
    • Protein or peptide: Histone H3Kc27me3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B

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Supramolecule #1: Human PRC1.4 bound to a H3Kc27me3 mononucleosome

SupramoleculeName: Human PRC1.4 bound to a H3Kc27me3 mononucleosome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#14
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Polyhomeotic-like protein 2, isoform B

MacromoleculeName: Polyhomeotic-like protein 2, isoform B / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GPDSMTSGNG NSASSIAGTA PQNGENKPPQ AIVKPQILTH VIEGFVIQEG AEPFPVGRSS LLVGNLKKKY AQGFLPEKLP QQDHTTTTDS EMEEPYLQES KEEGAPLKLK CELCGRVDFA YKFKRSKRFC SMACAKRYNV GCTKRVGLFH SDRSKLQKAG AATHNRRRAS ...String:
GPDSMTSGNG NSASSIAGTA PQNGENKPPQ AIVKPQILTH VIEGFVIQEG AEPFPVGRSS LLVGNLKKKY AQGFLPEKLP QQDHTTTTDS EMEEPYLQES KEEGAPLKLK CELCGRVDFA YKFKRSKRFC SMACAKRYNV GCTKRVGLFH SDRSKLQKAG AATHNRRRAS KASLPPLTKD TKKQPTGTVP LSVTAALQLT HSQEDSSRCS DNSSYEEPLS PISASSSTSR RRQGQRDLEL PDMHMRDLVG MGHHFLPSEP TKWNVEDVYE FIRSLPGCQE IAEEFRAQEI DGQALLLLKE DHLMSAMNIE LGPALEIYAR ISMLKDS

UniProtKB: Isoform 2 of Polyhomeotic-like protein 2

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Macromolecule #2: Chromobox 7

MacromoleculeName: Chromobox 7 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
GPDSMELSAI GEQVFAVESI RKKRVRKGKV EYLVKWKGWP PKYSTWEPEE HILDPRLVMA YEEKEERDRA SGYRKRGPKP KRLLLQEPP APDVLQAAGE WEPAAQPPEE EADADLAEGP PPWTPALPSS EVTVTDITAN SITVTFREAQ AAEGFFRDRS G KF

UniProtKB: Chromobox 7

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Macromolecule #3: E3 ubiquitin-protein ligase RING2

MacromoleculeName: E3 ubiquitin-protein ligase RING2 / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GPDSMSQAVQ TNGTQPLSKT WELSLYELQR TPQEAITDGL EIVVSPRSLH SELMCPICLD MLKNTMTTKE CLHRFCADCI ITALRSGNK ECPTCRKKLV SKRSLRPDPN FDALISKIYP SRDEYEAHQE RVLARINKHN NQQALSHSIE EGLKIQAMNR L QRGKKQQI ...String:
GPDSMSQAVQ TNGTQPLSKT WELSLYELQR TPQEAITDGL EIVVSPRSLH SELMCPICLD MLKNTMTTKE CLHRFCADCI ITALRSGNK ECPTCRKKLV SKRSLRPDPN FDALISKIYP SRDEYEAHQE RVLARINKHN NQQALSHSIE EGLKIQAMNR L QRGKKQQI ENGSGAEDNG DSSHCSNAST HSNQEAGPSN KRTKTSDDSG LELDNNNAAM AIDPVMDGAS EIELVFRPHP TL MEKDDSA QTRYIKTSGN ATVDHLSKYL AVRLALEELR SKGESNQMNL DTASEKQYTI YIATASGQFT VLNGSFSLEL VSE KYWKVN KPMELYYAPT KEHK

UniProtKB: E3 ubiquitin-protein ligase RING2

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Macromolecule #4: Polycomb complex protein BMI-1

MacromoleculeName: Polycomb complex protein BMI-1 / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV HKTRPLLNIR SDKTLQDIVY KLVPGLFKN EMKRRRDFYA AHPSADAANG SNEDRGEVAD EDKRIITDDE IISLSIEFFD QNRLDRKVNK DKEKSKEEVN D KRYLRCPA ...String:
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK TCIVRYLETS KYCPICDVQV HKTRPLLNIR SDKTLQDIVY KLVPGLFKN EMKRRRDFYA AHPSADAANG SNEDRGEVAD EDKRIITDDE IISLSIEFFD QNRLDRKVNK DKEKSKEEVN D KRYLRCPA AMTVMHLRKF LRSKMDIPNT FQIDVMYEEE PLKDYYTLMD IAYIYTWRRN GPLPLKYRVR PTCKRMKISH QR DGLTNAG ELESDSGSDK ANSPAGGIPS TSSCLPSPST PVQSPHPQFP HISSTMNGTS NSPSGNHQSS FANRPRKSSV NGS SATSSG GSGSLEVLFQ

UniProtKB: Polycomb complex protein BMI-1

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Macromolecule #5: Histone H3Kc27me3

MacromoleculeName: Histone H3Kc27me3 / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
ARTKQTARKS TGGKAPRKQL ATKAARK(ME3)SA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIA QDF KTDLRFQSSA VMALQEASEA YLVALFEDTN LAAIHAKRVT IMPKDIQLAR RIRGERA

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Macromolecule #6: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYAL KRQGRTLYGF GG

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Macromolecule #7: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKQGGKT RAKAKTRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAVRND EELNKLLGRV TIAQGGVLPN IQSVLLPKKT ESSKSAKSK

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Macromolecule #8: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
AKSAPAPKKG SKKAVTKTQK KDGKKRRKTR KESYAIYVYK VLKQVHPDTG ISSKAMSIMN SFVNDVFERI AGEASRLAHY NKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT SAK

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Macromolecule #11: Histone H3Kc27me3

MacromoleculeName: Histone H3Kc27me3 / type: protein_or_peptide / ID: 11 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
ARTKQTARKS TGGKAPRKQL ATKAARK(ME3)SA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIA QDF KTDLRFQSSA VMALQEASEA YLVALFEDTN LAAIHAKRVT IMPKDIQLAR RIRGERA

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Macromolecule #12: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 12 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYAL KRQGRTLYGF GG

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Macromolecule #13: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 13 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKQGGKT RAKAKTRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAVRND EELNKLLGRV TIAQGGVLPN IQSVLLPKKT ESSKSAKSK

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Macromolecule #14: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 14 / Enantiomer: LEVO
Source (natural)Organism: Xenopus (frog)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
AKSAPAPKKG SKKAVTKTQK KDGKKRRKTR KESYAIYVYK VLKQVHPDTG ISSKAMSIMN SFVNDVFERI AGEASRLAHY NKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT SAK

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Macromolecule #9: DNA (151-MER)

MacromoleculeName: DNA (151-MER) / type: dna / ID: 9 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
SequenceString: (DA)(DT)(DA)(DT)(DC)(DT)(DC)(DG)(DG)(DG) (DC)(DT)(DT)(DA)(DT)(DG)(DT)(DG)(DA)(DT) (DG)(DG)(DA)(DC)(DC)(DC)(DT)(DA)(DT) (DA)(DC)(DG)(DC)(DG)(DG)(DC)(DG)(DG)(DA) (DC) (DC)(DT)(DG)(DG)(DA)(DG) ...String:
(DA)(DT)(DA)(DT)(DC)(DT)(DC)(DG)(DG)(DG) (DC)(DT)(DT)(DA)(DT)(DG)(DT)(DG)(DA)(DT) (DG)(DG)(DA)(DC)(DC)(DC)(DT)(DA)(DT) (DA)(DC)(DG)(DC)(DG)(DG)(DC)(DG)(DG)(DA) (DC) (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA) (DT)(DC)(DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC) (DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT) (DC)(DA)(DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG) (DT)(DA)(DG) (DA)(DC)(DA)(DG)(DC)(DT) (DC)(DT)(DA)(DG)(DC)(DA)(DC)(DC)(DG)(DC) (DT)(DT)(DA)(DA) (DA)(DC)(DG)(DC)(DA) (DC)(DG)(DT)(DA)(DC)(DG)(DC)(DG)(DC)(DT) (DG)(DT)(DC)(DC)(DC) (DC)(DC)(DG)(DC) (DG)(DT)(DT)(DT)(DT)(DA)(DA)(DC)(DC)(DG) (DC)(DC)(DA)(DA)(DG)(DG) (DG)(DG)(DA) (DT)(DT)(DA)(DC)(DT)(DC)(DC)(DC)(DT)(DA) (DG)(DT)(DC)(DT)(DC)(DC)(DA) (DG)(DG) (DC)(DA)(DC)(DG)(DT)(DG)(DT)(DC)(DA)(DG) (DA)(DT)(DA)(DT)(DA)(DT)(DA)(DC) (DA) (DT)(DC)(DC)(DT)(DG)(DT)(DG)(DT)(DA)(DT) (DT)(DT)(DA)(DT)(DT)(DG)(DA)(DA)(DC) (DA)(DG)(DC)(DG)(DA)(DC)(DT)(DC)(DG)(DG) (DG)(DA)(DT)(DA)(DT)(DC)(DT)(DC)(DT)(DA) (DG)(DA)(DG)(DT)(DC)(DG)(DA)(DC)(DC) (DT)(DG)(DC)(DA)(DG)(DG)(DC)(DA)(DT)(DG) (DC) (DA)(DA)(DG)(DC)(DT)(DT)(DG)(DG)

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Macromolecule #10: DNA (151-MER)

MacromoleculeName: DNA (151-MER) / type: dna / ID: 10 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
SequenceString: (DC)(DC)(DA)(DA)(DG)(DC)(DT)(DT)(DG)(DC) (DA)(DT)(DG)(DC)(DC)(DT)(DG)(DC)(DA)(DG) (DG)(DT)(DC)(DG)(DA)(DC)(DT)(DC)(DT) (DA)(DG)(DA)(DG)(DA)(DT)(DA)(DT)(DC)(DC) (DC) (DG)(DA)(DG)(DT)(DC)(DG) ...String:
(DC)(DC)(DA)(DA)(DG)(DC)(DT)(DT)(DG)(DC) (DA)(DT)(DG)(DC)(DC)(DT)(DG)(DC)(DA)(DG) (DG)(DT)(DC)(DG)(DA)(DC)(DT)(DC)(DT) (DA)(DG)(DA)(DG)(DA)(DT)(DA)(DT)(DC)(DC) (DC) (DG)(DA)(DG)(DT)(DC)(DG)(DC)(DT) (DG)(DT)(DT)(DC)(DA)(DA)(DT)(DA)(DA)(DA) (DT)(DA) (DC)(DA)(DC)(DA)(DG)(DG)(DA) (DT)(DG)(DT)(DA)(DT)(DA)(DT)(DA)(DT)(DC) (DT)(DG)(DA) (DC)(DA)(DC)(DG)(DT)(DG) (DC)(DC)(DT)(DG)(DG)(DA)(DG)(DA)(DT)(DT) (DA)(DG)(DG)(DG) (DA)(DG)(DT)(DA)(DA) (DT)(DC)(DC)(DC)(DC)(DT)(DT)(DG)(DG)(DC) (DG)(DG)(DT)(DT)(DA) (DA)(DA)(DA)(DC) (DG)(DC)(DG)(DG)(DG)(DG)(DG)(DA)(DC)(DA) (DG)(DC)(DG)(DC)(DG)(DT) (DA)(DC)(DG) (DT)(DG)(DC)(DG)(DT)(DT)(DT)(DA)(DA)(DG) (DC)(DG)(DG)(DT)(DG)(DC)(DT) (DA)(DG) (DA)(DG)(DC)(DT)(DG)(DT)(DC)(DT)(DA)(DC) (DG)(DA)(DC)(DC)(DA)(DA)(DT)(DT) (DG) (DA)(DG)(DC)(DG)(DG)(DC)(DC)(DT)(DC)(DG) (DG)(DC)(DA)(DC)(DC)(DG)(DG)(DG)(DA) (DT)(DT)(DC)(DT)(DC)(DC)(DA)(DG)(DG)(DT) (DC)(DC)(DG)(DC)(DC)(DG)(DC)(DG)(DT)(DA) (DT)(DA)(DG)(DG)(DG)(DT)(DC)(DC)(DA) (DT)(DC)(DA)(DC)(DA)(DT)(DA)(DA)(DG)(DC) (DC) (DC)(DG)(DA)(DG)(DA)(DT)(DA)(DT)

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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: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 55.8 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.5 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: NONE / Details: Ab intio
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.72 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 33810
Initial angle assignmentType: RANDOM ASSIGNMENT
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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