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- EMDB-34274: Bre1-nucleosome complex -

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Basic information

Entry
Database: EMDB / ID: EMD-34274
TitleBre1-nucleosome complex
Map data3DFlex map
Sample
  • Complex: Bre1-nucleosome complex
    • Complex: Histone
      • Protein or peptide: Histone H3.1
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
      • Protein or peptide: Histone H2B type 1-J
    • Complex: DNA
      • DNA: DNA (147-mer)
      • DNA: DNA (147-mer)
    • Complex: Bre1
      • Protein or peptide: E3 ubiquitin-protein ligase BRE1A
      • Protein or peptide: E3 ubiquitin-protein ligase BRE1B
  • Ligand: ZINC ION
Keywordstranscription / ubiquitin ligase / cancer / chromatin / GENE REGULATION / GENE REGULATION-DNA complex
Function / homology
Function and homology information


histone H2B C-terminal K residue ubiquitin ligase activity / HULC complex / RHOBTB1 GTPase cycle / negative regulation of tumor necrosis factor-mediated signaling pathway / ubiquitin ligase complex / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome ...histone H2B C-terminal K residue ubiquitin ligase activity / HULC complex / RHOBTB1 GTPase cycle / negative regulation of tumor necrosis factor-mediated signaling pathway / ubiquitin ligase complex / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Deposition of new CENPA-containing nucleosomes at the centromere / telomere organization / Inhibition of DNA recombination at telomere / Meiotic synapsis / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / innate immune response in mucosa / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / negative regulation of cell migration / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / SIRT1 negatively regulates rRNA expression / epigenetic regulation of gene expression / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / mRNA 3'-UTR binding / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / Nonhomologous End-Joining (NHEJ) / RNA Polymerase I Promoter Escape / lipopolysaccharide binding / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / HDMs demethylate histones / NoRC negatively regulates rRNA expression / RING-type E3 ubiquitin transferase / DNA Damage/Telomere Stress Induced Senescence / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / Metalloprotease DUBs / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / HCMV Early Events / antimicrobial humoral immune response mediated by antimicrobial peptide / protein polyubiquitination / ubiquitin-protein transferase activity / structural constituent of chromatin / antibacterial humoral response / p53 binding / UCH proteinases / ubiquitin protein ligase activity / nucleosome / heterochromatin formation / E3 ubiquitin ligases ubiquitinate target proteins / nucleosome assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / HATs acetylate histones / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / Processing of DNA double-strand break ends / Senescence-Associated Secretory Phenotype (SASP) / ubiquitin-dependent protein catabolic process / defense response to Gram-negative bacterium / Oxidative Stress Induced Senescence / gene expression / killing of cells of another organism / Estrogen-dependent gene expression / histone binding / transcription coactivator activity / chromosome, telomeric region / defense response to Gram-positive bacterium / neuron projection / Ub-specific processing proteases / protein ubiquitination / cadherin binding / Amyloid fiber formation / protein heterodimerization activity / ubiquitin protein ligase binding / chromatin binding / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription
Similarity search - Function
E3 ubiquitin ligase Bre1 / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / : / Histone H2B signature. / Histone H2B / Histone H2B ...E3 ubiquitin ligase Bre1 / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / : / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Histone H3 signature 1. / Zinc finger RING-type profile. / Zinc finger, RING-type / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Zinc finger, RING/FYVE/PHD-type
Similarity search - Domain/homology
E3 ubiquitin-protein ligase BRE1B / Histone H2B type 1-J / Histone H2A type 1 / Histone H4 / Histone H3.1 / E3 ubiquitin-protein ligase BRE1A
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.81 Å
AuthorsOnishi S / Hamada K / Sato K / Nishizawa T / Nureki O / Ogata K / Sengoku T
Funding support Japan, 1 items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS) Japan
CitationJournal: Nat Commun / Year: 2024
Title: Structure of the human Bre1 complex bound to the nucleosome.
Authors: Shuhei Onishi / Kotone Uchiyama / Ko Sato / Chikako Okada / Shunsuke Kobayashi / Keisuke Hamada / Tomohiro Nishizawa / Osamu Nureki / Kazuhiro Ogata / Toru Sengoku /
Abstract: Histone H2B monoubiquitination (at Lys120 in humans) regulates transcription elongation and DNA repair. In humans, H2B monoubiquitination is catalyzed by the heterodimeric Bre1 complex composed of ...Histone H2B monoubiquitination (at Lys120 in humans) regulates transcription elongation and DNA repair. In humans, H2B monoubiquitination is catalyzed by the heterodimeric Bre1 complex composed of Bre1A/RNF20 and Bre1B/RNF40. The Bre1 proteins generally function as tumor suppressors, while in certain cancers, they facilitate cancer cell proliferation. To obtain structural insights of H2BK120 ubiquitination and its regulation, we report the cryo-electron microscopy structure of the human Bre1 complex bound to the nucleosome. The two RING domains of Bre1A and Bre1B recognize the acidic patch and the nucleosomal DNA phosphates around SHL 6.0-6.5, which are ideally located to recruit the E2 enzyme and ubiquitin for H2BK120-specific ubiquitination. Mutational experiments suggest that the two RING domains bind in two orientations and that ubiquitination occurs when Bre1A binds to the acidic patch. Our results provide insights into the H2BK120-specific ubiquitination by the Bre1 proteins and suggest that H2B monoubiquitination can be regulated by nuclesomal DNA flexibility.
History
DepositionSep 12, 2022-
Header (metadata) releaseSep 20, 2023-
Map releaseSep 20, 2023-
UpdateApr 3, 2024-
Current statusApr 3, 2024Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_34274.png

Downloads & links

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Map

FileDownload / File: emd_34274.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotation3DFlex map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 320 pix.
= 336. Å		1.05 Å/pix.
x 320 pix.
= 336. Å		1.05 Å/pix.
x 320 pix.
= 336. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.05 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.006
Minimum - Maximum-0.017542299 - 0.043336485
Average (Standard dev.)0.00004297897 (±0.0008172334)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 336.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: NU-refinement map

Fileemd_34274_additional_1.map
AnnotationNU-refinement map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: 3DFlex half map

Fileemd_34274_half_map_1.map
Annotation3DFlex half map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: 3DFlex half map

Fileemd_34274_half_map_2.map
Annotation3DFlex half map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Bre1-nucleosome complex

EntireName: Bre1-nucleosome complex
Components
  • Complex: Bre1-nucleosome complex
    • Complex: Histone
      • Protein or peptide: Histone H3.1
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1
      • Protein or peptide: Histone H2B type 1-J
    • Complex: DNA
      • DNA: DNA (147-mer)
      • DNA: DNA (147-mer)
    • Complex: Bre1
      • Protein or peptide: E3 ubiquitin-protein ligase BRE1A
      • Protein or peptide: E3 ubiquitin-protein ligase BRE1B
  • Ligand: ZINC ION

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Supramolecule #1: Bre1-nucleosome complex

SupramoleculeName: Bre1-nucleosome complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#8

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Supramolecule #2: Histone

SupramoleculeName: Histone / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#4
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: DNA

SupramoleculeName: DNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #5-#6

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Supramolecule #4: Bre1

SupramoleculeName: Bre1 / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #7-#8
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Histone H3.1

MacromoleculeName: Histone H3.1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.437167 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEACEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.1

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Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.263231 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYA LKRQGRTLYG FGG

UniProtKB: Histone H4

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Macromolecule #3: Histone H2A type 1

MacromoleculeName: Histone H2A type 1 / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.990342 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKQGGKA RAKAKTRSSR AGLQFPVGRV HRLLRKGNYA ERVGAGAPVY LAAVLEYLTA EILELAGNAA RDNKKTRIIP RHLQLAIRN DEELNKLLGK VTIAQGGVLP NIQAVLLPKK TESHHKAKGK

UniProtKB: Histone H2A type 1

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Macromolecule #4: Histone H2B type 1-J

MacromoleculeName: Histone H2B type 1-J / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.217516 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSHMPEPAKS APAPKKGSKK AVTKAQKKDG KKRKRSRKES YSIYVYKVLK QVHPDTGISS KAMGIMNSFV NDIFERIAGE ASRLAHYNK RSTITSREIQ TAVRLLLPGE LAKHAVSEGT KAVTKYTSAK

UniProtKB: Histone H2B type 1-J

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Macromolecule #7: E3 ubiquitin-protein ligase BRE1A

MacromoleculeName: E3 ubiquitin-protein ligase BRE1A / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 113.86182 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSGIGNKRAA GEPGTSMPPE KKAAVEDSGT TVETIKLGGV SSTEELDIRT LQTKNRKLAE MLDQRQAIED ELREHIEKLE RRQATDDAS LLIVNRYWSQ FDENIRIILK RYDLEQGLGD LLTERKALVV PEPEPDSDSN QERKDDRERG EGQEPAFSFL A TLASSSSE ...String:
MSGIGNKRAA GEPGTSMPPE KKAAVEDSGT TVETIKLGGV SSTEELDIRT LQTKNRKLAE MLDQRQAIED ELREHIEKLE RRQATDDAS LLIVNRYWSQ FDENIRIILK RYDLEQGLGD LLTERKALVV PEPEPDSDSN QERKDDRERG EGQEPAFSFL A TLASSSSE EMESQLQERV ESSRRAVSQI VTVYDKLQEK VELLSRKLNS GDNLIVEEAV QELNSFLAQE NMRLQELTDL LQ EKHRTMS QEFSKLQSKV ETAESRVSVL ESMIDDLQWD IDKIRKREQR LNRHLAEVLE RVNSKGYKVY GAGSSLYGGT ITI NARKFE EMNAELEENK ELAQNRLCEL EKLRQDFEEV TTQNEKLKVE LRSAVEQVVK ETPEYRCMQS QFSVLYNESL QLKA HLDEA RTLLHGTRGT HQHQVELIER DEVSLHKKLR TEVIQLEDTL AQVRKEYEML RIEFEQTLAA NEQAGPINRE MRHLI SSLQ NHNHQLKGEV LRYKRKLREA QSDLNKTRLR SGSALLQSQS STEDPKDEPA ELKPDSEDLS SQSSASKASQ EDANEI KSK RDEEERERER REKERERERE REKEKERERE KQKLKESEKE RDSAKDKEKG KHDDGRKKEA EIIKQLKIEL KKAQESQ KE MKLLLDMYRS APKEQRDKVQ LMAAEKKSKA ELEDLRQRLK DLEDKEKKEN KKMADEDALR KIRAVEEQIE YLQKKLAM A KQEEEALLSE MDVTGQAFED MQEQNIRLMQ QLREKDDANF KLMSERIKSN QIHKLLKEEK EELADQVLTL KTQVDAQLQ VVRKLEEKEH LLQSNIGTGE KELGLRTQAL EMNKRKAMEA AQLADDLKAQ LELAQKKLHD FQDEIVENSV TKEKDMFNFK RAQEDISRL RRKLETTKKP DNVPKCDEIL MEEIKDYKAR LTCPCCNMRK KDAVLTKCFH VFCFECVKTR YDTRQRKCPK C NAAFGAND FHRIYIG

UniProtKB: E3 ubiquitin-protein ligase BRE1A

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Macromolecule #8: E3 ubiquitin-protein ligase BRE1B

MacromoleculeName: E3 ubiquitin-protein ligase BRE1B / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 113.863906 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA ERLEQRQACE DELRERIEKL EKRQATDDA TLLIVNRYWA QLDETVEALL RCHESQGELS SAPEAPGTQE GPTCDGTPLP EPGTSELRDP LLMQLRPPLS E PALAFVVA ...String:
MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA ERLEQRQACE DELRERIEKL EKRQATDDA TLLIVNRYWA QLDETVEALL RCHESQGELS SAPEAPGTQE GPTCDGTPLP EPGTSELRDP LLMQLRPPLS E PALAFVVA LGASSSEEVE LELQGRMEFS KAAVSRVVEA SDRLQRRVEE LCQRVYSRGD SEPLSEAAQA HTRELGRENR RL QDLATQL QEKHHRISLE YSELQDKVTS AETKVLEMET TVEDLQWDIE KLRKREQKLN KHLAEALEQL NSGYYVSGSS SGF QGGQIT LSMQKFEMLN AELEENQELA NSRMAELEKL QAELQGAVRT NERLKVALRS LPEEVVRETG EYRMLQAQFS LLYN ESLQV KTQLDEARGL LLATKNSHLR HIEHMESDEL GLQKKLRTEV IQLEDTLAQV RKEYEMLRIE FEQNLAANEQ AGPIN REMR HLISSLQNHN HQLKGDAQRY KRKLREVQAE IGKLRAQASG SAHSTPNLGH PEDSGVSAPA PGKEEGGPGP VSTPDN RKE MAPVPGTTTT TTSVKKEELV PSEEDFQGIT PGAQGPSSRG REPEARPKRE LREREGPSLG PPPVASALSR ADREKAK VE ETKRKESELL KGLRAELKKA QESQKEMKLL LDMYKSAPKE QRDKVQLMAA ERKAKAEVDE LRSRIRELEE RDRRESKK I ADEDALRRIR QAEEQIEHLQ RKLGATKQEE EALLSEMDVT GQAFEDMQEQ NGRLLQQLRE KDDANFKLMS ERIKANQIH KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQP CLAESRAARE KESFNLKRAQ EDISRLRRKL EKQRKVEVYA DADEILQEEI KEYKARLTCP CCNTRKKDAV L TKCFHVFC FECVRGRYEA RQRKCPKCNA AFGAHDFHRI YIS

UniProtKB: E3 ubiquitin-protein ligase BRE1B

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Macromolecule #5: DNA (147-mer)

MacromoleculeName: DNA (147-mer) / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 45.145754 KDa
SequenceString: (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) ...String:
(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)

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Macromolecule #6: DNA (147-mer)

MacromoleculeName: DNA (147-mer) / type: dna / ID: 6 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 45.604047 KDa
SequenceString: (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)(DC)(DT)(DA)(DG)(DG)(DG) (DA) (DG)(DT)(DA)(DA)(DT)(DC) ...String:
(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)(DC)(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)

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Macromolecule #9: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 9 / Number of copies: 4 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 58.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.81 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 83000
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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