9mu4

Structure of a native Drosophila melanogaster octameric nucleosome

Method: ELECTRON MICROSCOPY Dmax: 141.0 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Histone H2A

OrganismNot specified

UniProt P84051

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain c; UniProt 14–119 Chain g; UniProt 14–119 Not recorded Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) DNA (164-MER) × 1 DNA (164-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM HEPES-HCl (pH = 7.5), 150 mM NaCl, 5% glycerol, 1 mM EDTA, 350 ug/mL 3x FLAG peptide, 1/1000th protease inhibitor cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2A_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain c; PDBConstruct 1–106; UniProt 14–119 Author chain g; PDBConstruct 1–106; UniProt 14–119

Histone H2B

OrganismNot specified

UniProt P02283

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain d; UniProt 27–123 Chain h; UniProt 27–123 Not recorded Histone H2A × 2 (P84051) Histone H3 × 2 (P02299) Histone H4 × 2 (P84040) DNA (164-MER) × 1 DNA (164-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM HEPES-HCl (pH = 7.5), 150 mM NaCl, 5% glycerol, 1 mM EDTA, 350 ug/mL 3x FLAG peptide, 1/1000th protease inhibitor cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

21 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B_DROME
Isoform
PDB entities 2
Chains and sequence ranges Author chain d; PDBConstruct 1–97; UniProt 27–123 Author chain h; PDBConstruct 1–97; UniProt 27–123

Histone H3

OrganismNot specified

UniProt P02299

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain a; UniProt 37–136 Chain e; UniProt 37–136 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H4 × 2 (P84040) DNA (164-MER) × 1 DNA (164-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM HEPES-HCl (pH = 7.5), 150 mM NaCl, 5% glycerol, 1 mM EDTA, 350 ug/mL 3x FLAG peptide, 1/1000th protease inhibitor cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

23 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3_DROME
Isoform
PDB entities 3
Chains and sequence ranges Author chain a; PDBConstruct 1–100; UniProt 37–136 Author chain e; PDBConstruct 1–100; UniProt 37–136

Histone H4

OrganismNot specified

UniProt P84040

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–DNA Heteromer Protein × 8 DNA 2 PDB declaration: decameric(10) Consistent with all polymer counts Chain b; UniProt 22–103 Chain f; UniProt 22–103 Not recorded Histone H2A × 2 (P84051) Histone H2B × 2 (P02283) Histone H3 × 2 (P02299) DNA (164-MER) × 1 DNA (164-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;10 mM HEPES-HCl (pH = 7.5), 150 mM NaCl, 5% glycerol, 1 mM EDTA, 350 ug/mL 3x FLAG peptide, 1/1000th protease inhibitor cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.29 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

18 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_DROME
Isoform
PDB entities 4
Chains and sequence ranges Author chain b; PDBConstruct 1–82; UniProt 22–103 Author chain f; PDBConstruct 1–82; UniProt 22–103

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9mu4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9mu4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9mu4
Deposition date deposition_date2025-01-13
最后修订 last_revision2025-02-19
Structure title titleStructure of a native Drosophila melanogaster octameric nucleosome
Keywords keywordsNucleosome, histones, histone, chromatin, DNA, GENE REGULATION; GENE REGULATION
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier43.07
Radius of gyration Rg (electron density) rg_electron40.34
Forward intensity I(0) i0968651000.00
Molecular weight molecular_weight187900.0 kDa
Excluded volume excluded_volume206840 ų
Envelope volume envelope_volume323960 ų
Hydration-shell volume shell_volume66234 ų
Envelope diameter envelope_diameter151.4
Shell Rg shell_rg46.62
Envelope Rg envelope_rg40.47
Shape Rg shape_rg40.16
Total Rg total_rg40.99
Total atoms total_atoms12794
Residues n_residues1098
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax141.0
Rg (real space) rg_real43.01
Rg uncertainty (real space) rg_real_error1.25
I(0) (real space) i0_real9.6860e+08
I(0) uncertainty (real space) i0_real_error1.8670e+07
Rg (reciprocal space) rg_reciprocal43.07
I(0) (reciprocal space) i0_reciprocal968700000.0000
Solution quality estimate total_estimate0.6586
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.262
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha73240000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.878; Stabil: 1.000; Sysdev: 0.083; Positv: 1.000; Valcen: 0.993; Smooth: 0.679

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)