8j91

Cryo-EM structure of nucleosome containing Arabidopsis thaliana histones

Method: ELECTRON MICROSCOPY Dmax: 111.1 Å Quality: GOOD

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

Histone H3.1

Arabidopsis thaliana

UniProt P59226

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 1–136 Chain E; UniProt 1–136 Not recorded Histone H4 × 2 (P59259) HTA13 × 2 (Q9LHQ5) Histone H2B.6 × 2 (O23629) DNA (169-MER) × 1 DNA (169-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

36 other PDB entries and 47 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H31_ARATH
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–139; UniProt 1–136 Author chain E; PDBConstruct 4–139; UniProt 1–136

Histone H4

Arabidopsis thaliana

UniProt P59259

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 1–103 Chain F; UniProt 1–103 Not recorded Histone H3.1 × 2 (P59226) HTA13 × 2 (Q9LHQ5) Histone H2B.6 × 2 (O23629) DNA (169-MER) × 1 DNA (169-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H4_ARATH
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 4–106; UniProt 1–103 Author chain F; PDBConstruct 4–106; UniProt 1–103

HTA13

Arabidopsis thaliana

UniProt Q9LHQ5

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 1–132 Chain G; UniProt 1–132 Not recorded Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) Histone H2B.6 × 2 (O23629) DNA (169-MER) × 1 DNA (169-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name H2A2_ARATH
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 4–135; UniProt 1–132 Author chain G; PDBConstruct 4–135; UniProt 1–132

Histone H2B.6

Arabidopsis thaliana

UniProt O23629

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 1–150 Chain H; UniProt 1–150 Not recorded Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) HTA13 × 2 (Q9LHQ5) DNA (169-MER) × 1 DNA (169-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B6_ARATH
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 4–153; UniProt 1–150 Author chain H; PDBConstruct 4–153; UniProt 1–150

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 8j91

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8j91
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8j91
Deposition date deposition_date2023-05-02
Structure title titleCryo-EM structure of nucleosome containing Arabidopsis thaliana histones
Keywords keywordsChromatin, Epigenetics, Histon variant, chromatin remodeler, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier38.63
Radius of gyration Rg (electron density) rg_electron35.73
Forward intensity I(0) i0553553000.00
Molecular weight molecular_weight145480.0 kDa
Excluded volume excluded_volume162920 ų
Envelope volume envelope_volume239610 ų
Hydration-shell volume shell_volume55579 ų
Envelope diameter envelope_diameter113.0
Shell Rg shell_rg42.70
Envelope Rg envelope_rg35.06
Shape Rg shape_rg35.55
Total Rg total_rg36.49
Total atoms total_atoms9944
Residues n_residues904
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 dmax111.1
Rg (real space) rg_real38.37
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real5.5360e+08
I(0) uncertainty (real space) i0_real_error8.7000e+06
Rg (reciprocal space) rg_reciprocal38.53
I(0) (reciprocal space) i0_reciprocal553600000.0000
Solution quality estimate total_estimate0.8778
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.0
Skewness Skewness skewness0.075
Kurtosis Kurtosis kurtosis-0.615
Angular range angular_range— – 0.2050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha18590000.0000
Real-space data points n_real_points42
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.987; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.456

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)