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- EMDB-10391: Structure of human Sox11 transcription factor in complex with a n... -

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Basic information

Entry
Database: EMDB / ID: EMD-10391
TitleStructure of human Sox11 transcription factor in complex with a nucleosome
Map dataStructure of human Sox11 transcription factor in complex with a nucleosome
Sample
  • Complex: Structure of human Sox11 transcription factor in complex with a nucleosome
    • Complex: Sox11 transcription factor, histones
      • Protein or peptide: Histone H3.2
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1-B/E
      • Protein or peptide: Histone H2B type 1-K
      • Protein or peptide: Transcription factor SOX-11
    • Complex: DNA
      • DNA: DNA (147-MER)
      • DNA: DNA (147-MER)
Function / homology
Function and homology information


closure of optic fissure / positive regulation of lens epithelial cell proliferation / soft palate development / cornea development in camera-type eye / positive regulation of hippo signaling / noradrenergic neuron differentiation / negative regulation of transcription regulatory region DNA binding / negative regulation of lymphocyte proliferation / hard palate development / lens morphogenesis in camera-type eye ...closure of optic fissure / positive regulation of lens epithelial cell proliferation / soft palate development / cornea development in camera-type eye / positive regulation of hippo signaling / noradrenergic neuron differentiation / negative regulation of transcription regulatory region DNA binding / negative regulation of lymphocyte proliferation / hard palate development / lens morphogenesis in camera-type eye / embryonic skeletal system morphogenesis / regulation of transforming growth factor beta receptor signaling pathway / embryonic digestive tract morphogenesis / neuroepithelial cell differentiation / oligodendrocyte development / sympathetic nervous system development / positive regulation of hormone secretion / positive regulation of BMP signaling pathway / positive regulation of ossification / positive regulation of neurogenesis / negative regulation of glial cell proliferation / spinal cord development / ventricular septum morphogenesis / lung morphogenesis / positive regulation of stem cell proliferation / eyelid development in camera-type eye / outflow tract morphogenesis / skeletal muscle cell differentiation / anatomical structure morphogenesis / positive regulation of osteoblast differentiation / glial cell proliferation / 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 / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / positive regulation of neuron differentiation / telomere organization / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / SUMOylation of chromatin organization proteins / Assembly of the ORC complex at the origin of replication / DNA methylation / Condensation of Prophase Chromosomes / HCMV Late Events / Chromatin modifications during the maternal to zygotic transition (MZT) / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / innate immune response in mucosa / PRC2 methylates histones and DNA / kidney development / Defective pyroptosis / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Nonhomologous End-Joining (NHEJ) / 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 / NoRC negatively regulates rRNA expression / G2/M DNA damage checkpoint / B-WICH complex positively regulates rRNA expression / HDMs demethylate histones / DNA Damage/Telomere Stress Induced Senescence / Metalloprotease DUBs / neuron differentiation / PKMTs methylate histone lysines / RMTs methylate histone arginines / Meiotic recombination / Pre-NOTCH Transcription and Translation / nucleosome assembly / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / UCH proteinases / nucleosome / antimicrobial humoral immune response mediated by antimicrobial peptide / E3 ubiquitin ligases ubiquitinate target proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / RUNX1 regulates transcription of genes involved in differentiation of HSCs / nervous system development / chromatin organization / Factors involved in megakaryocyte development and platelet production / Processing of DNA double-strand break ends / HATs acetylate histones / antibacterial humoral response / Senescence-Associated Secretory Phenotype (SASP) / DNA-binding transcription activator activity, RNA polymerase II-specific / Oxidative Stress Induced Senescence / killing of cells of another organism / Estrogen-dependent gene expression
Similarity search - Function
Transcription factor SOX-12/11/4 / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site ...Transcription factor SOX-12/11/4 / HMG (high mobility group) box / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / 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 / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold
Similarity search - Domain/homology
Histone H2B type 1-K / Histone H2A type 1-B/E / Transcription factor SOX-11 / Histone H4 / Histone H3.2
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsDodonova SO / Zhu F / Dienemann C / Taipale J / Cramer P
Funding support Germany, 3 items
OrganizationGrant numberCountry
European Research Council (ERC)693023 Germany
Volkswagen Foundation Germany
European Molecular Biology Organization (EMBO)ALTF-949-2016 Germany
CitationJournal: Nature / Year: 2020
Title: Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.
Authors: Svetlana O Dodonova / Fangjie Zhu / Christian Dienemann / Jussi Taipale / Patrick Cramer /
Abstract: 'Pioneer' transcription factors are required for stem-cell pluripotency, cell differentiation and cell reprogramming. Pioneer factors can bind nucleosomal DNA to enable gene expression from regions ...'Pioneer' transcription factors are required for stem-cell pluripotency, cell differentiation and cell reprogramming. Pioneer factors can bind nucleosomal DNA to enable gene expression from regions of the genome with closed chromatin. SOX2 is a prominent pioneer factor that is essential for pluripotency and self-renewal of embryonic stem cells. Here we report cryo-electron microscopy structures of the DNA-binding domains of SOX2 and its close homologue SOX11 bound to nucleosomes. The structures show that SOX factors can bind and locally distort DNA at superhelical location 2. The factors also facilitate detachment of terminal nucleosomal DNA from the histone octamer, which increases DNA accessibility. SOX-factor binding to the nucleosome can also lead to a repositioning of the N-terminal tail of histone H4 that includes residue lysine 16. We speculate that this repositioning is incompatible with higher-order nucleosome stacking, which involves contacts of the H4 tail with a neighbouring nucleosome. Our results indicate that pioneer transcription factors can use binding energy to initiate chromatin opening, and thereby facilitate nucleosome remodelling and subsequent transcription.
History
DepositionOct 21, 2019-
Header (metadata) releaseOct 30, 2019-
Map releaseApr 29, 2020-
UpdateDec 2, 2020-
Current statusDec 2, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6t7a
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10391.png

Downloads & links

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Map

FileDownload / File: emd_10391.map.gz / Format: CCP4 / Size: 10.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationStructure of human Sox11 transcription factor in complex with a nucleosome
Voxel sizeX=Y=Z: 1.05 Å
Density
Contour LevelBy AUTHOR: 0.04 / Movie #1: 0.04
Minimum - Maximum-0.12982592 - 0.2580135
Average (Standard dev.)0.0028442089 (±0.02100797)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions140140140
Spacing140140140
CellA=B=C: 147.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.051.051.05
M x/y/z140140140
origin x/y/z0.0000.0000.000
length x/y/z147.000147.000147.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ350350350
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS140140140
D min/max/mean-0.1300.2580.003

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Supplemental data

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Half map: half map 1

Fileemd_10391_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_10391_half_map_2.map
Annotationhalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Structure of human Sox11 transcription factor in complex with a n...

EntireName: Structure of human Sox11 transcription factor in complex with a nucleosome
Components
  • Complex: Structure of human Sox11 transcription factor in complex with a nucleosome
    • Complex: Sox11 transcription factor, histones
      • Protein or peptide: Histone H3.2
      • Protein or peptide: Histone H4
      • Protein or peptide: Histone H2A type 1-B/E
      • Protein or peptide: Histone H2B type 1-K
      • Protein or peptide: Transcription factor SOX-11
    • Complex: DNA
      • DNA: DNA (147-MER)
      • DNA: DNA (147-MER)

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Supramolecule #1: Structure of human Sox11 transcription factor in complex with a n...

SupramoleculeName: Structure of human Sox11 transcription factor in complex with a nucleosome
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#7
Molecular weightTheoretical: 218 KDa

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Supramolecule #2: Sox11 transcription factor, histones

SupramoleculeName: Sox11 transcription factor, histones / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#4, #7
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Supramolecule #3: DNA

SupramoleculeName: DNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #5-#6
Source (natural)Organism: synthetic construct (others)
Recombinant expressionOrganism: synthetic construct (others)

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Macromolecule #1: Histone H3.2

MacromoleculeName: Histone H3.2 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.389036 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVGLFEDTN LAAIHAKRVT IMPKDIQLAR RIRGERA

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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: 11.394426 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

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Macromolecule #3: Histone H2A type 1-B/E

MacromoleculeName: Histone H2A type 1-B/E / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.707277 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MGSSHHHHHH ENLYFQSNAP WMSGRGKQGG KARAKAKTRS SRAGLQFPVG RVHRLLRKGN YSERVGAGAP VYLAAVLEYL TAEILELAG NAARDNKKTR IIPRHLQLAI RNDEELNKLL GRVTIAQGGV LPNIQAVLLP KKTESHHKAK GK

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Macromolecule #4: Histone H2B type 1-K

MacromoleculeName: Histone H2B type 1-K / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.921213 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSAK

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Macromolecule #7: Transcription factor SOX-11

MacromoleculeName: Transcription factor SOX-11 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.856941 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SNAALDESDP DWCKTASGHI KRPMNAFMVW SKIERRKIME QSPDMHNAEI SKRLGKRWKM LKDSEKIPFI REAERLRLKH MADYPDYKY RPRKKPKMDP SAKPSASQSP

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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: 45.240848 KDa
SequenceString: (DA)(DT)(DC)(DT)(DA)(DC)(DA)(DC)(DG)(DA) (DC)(DG)(DC)(DT)(DC)(DT)(DT)(DC)(DC)(DG) (DA)(DT)(DC)(DT)(DA)(DA)(DT)(DT)(DT) (DA)(DT)(DG)(DT)(DT)(DT)(DG)(DT)(DT)(DA) (DG) (DC)(DG)(DT)(DT)(DA)(DT) ...String:
(DA)(DT)(DC)(DT)(DA)(DC)(DA)(DC)(DG)(DA) (DC)(DG)(DC)(DT)(DC)(DT)(DT)(DC)(DC)(DG) (DA)(DT)(DC)(DT)(DA)(DA)(DT)(DT)(DT) (DA)(DT)(DG)(DT)(DT)(DT)(DG)(DT)(DT)(DA) (DG) (DC)(DG)(DT)(DT)(DA)(DT)(DA)(DC) (DT)(DA)(DT)(DT)(DC)(DT)(DA)(DA)(DT)(DT) (DC)(DT) (DT)(DT)(DG)(DT)(DT)(DT)(DC) (DG)(DG)(DT)(DG)(DG)(DT)(DA)(DT)(DT)(DG) (DT)(DT)(DT) (DA)(DT)(DT)(DT)(DT)(DG) (DT)(DT)(DC)(DC)(DT)(DT)(DT)(DG)(DT)(DG) (DC)(DG)(DT)(DT) (DC)(DA)(DG)(DC)(DT) (DT)(DA)(DA)(DT)(DG)(DC)(DC)(DT)(DA)(DA) (DC)(DG)(DA)(DC)(DA) (DC)(DT)(DC)(DG) (DG)(DA)(DG)(DA)(DT)(DC)(DG)(DG)(DA)(DA) (DG)(DA)(DG)(DC)(DA)(DC) (DA)(DC)(DG) (DT)(DG)(DA)(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: 45.484273 KDa
SequenceString: (DA)(DT)(DC)(DA)(DC)(DG)(DT)(DG)(DT)(DG) (DC)(DT)(DC)(DT)(DT)(DC)(DC)(DG)(DA)(DT) (DC)(DT)(DC)(DC)(DG)(DA)(DG)(DT)(DG) (DT)(DC)(DG)(DT)(DT)(DA)(DG)(DG)(DC)(DA) (DT) (DT)(DA)(DA)(DG)(DC)(DT) ...String:
(DA)(DT)(DC)(DA)(DC)(DG)(DT)(DG)(DT)(DG) (DC)(DT)(DC)(DT)(DT)(DC)(DC)(DG)(DA)(DT) (DC)(DT)(DC)(DC)(DG)(DA)(DG)(DT)(DG) (DT)(DC)(DG)(DT)(DT)(DA)(DG)(DG)(DC)(DA) (DT) (DT)(DA)(DA)(DG)(DC)(DT)(DG)(DA) (DA)(DC)(DG)(DC)(DA)(DC)(DA)(DA)(DA)(DG) (DG)(DA) (DA)(DC)(DA)(DA)(DA)(DA)(DT) (DA)(DA)(DA)(DC)(DA)(DA)(DT)(DA)(DC)(DC) (DA)(DC)(DC) (DG)(DA)(DA)(DA)(DC)(DA) (DA)(DA)(DG)(DA)(DA)(DT)(DT)(DA)(DG)(DA) (DA)(DT)(DA)(DG) (DT)(DA)(DT)(DA)(DA) (DC)(DG)(DC)(DT)(DA)(DA)(DC)(DA)(DA)(DA) (DC)(DA)(DT)(DA)(DA) (DA)(DT)(DT)(DA) (DG)(DA)(DT)(DC)(DG)(DG)(DA)(DA)(DG)(DA) (DG)(DC)(DG)(DT)(DC)(DG) (DT)(DG)(DT) (DA)(DG)(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

Concentration0.15 mg/mL
BufferpH: 7.5
Component:
ConcentrationNameFormula
20.0 mMHEPES
30.0 mMNaClSodium chloride
1.0 mMEDTAEthylenediaminetetraacetic acid
2.0 mMDTT
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.039 kPa / Details: 0.39 mB, 25 mA
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 289 K / Instrument: FEI VITROBOT MARK IV
Details: The sample was applied onto glow-discharged Quantifoil holey carbon grids. The grids were blotted from both sides for 5-10 seconds at 16*C in a chamber at 100% humidity and plunge-frozen ...Details: The sample was applied onto glow-discharged Quantifoil holey carbon grids. The grids were blotted from both sides for 5-10 seconds at 16*C in a chamber at 100% humidity and plunge-frozen into liquid ethane using a manual plunger..

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 130000
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 30 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
DetailsAt least 50% of the data were collected at 25* stage tilt in order to partially compensate for preferred orientation of particles on the grid, and to improve angular distribution.
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average electron dose: 1.125 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: Gctf
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 202142
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

6t79

RefinementSpace: REAL / Protocol: OTHER / Overall B value: 100
Output model

PDB-6t7a:
Structure of human Sox11 transcription factor in complex with a nucleosome

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