9k43

Cryo-EM structure of Arabidopsis thaliana H2A.Z-nucleosome with 147bp Widom 601 DNA (C2 symmetry)

Method: ELECTRON MICROSCOPY Dmax: 114.3 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) Probable histone H2A variant 3 × 2 (Q9C944) Histone H2B.1 × 2 (Q9LQQ4) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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 1–136; UniProt 1–136 Author chain E; PDBConstruct 1–136; 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) Probable histone H2A variant 3 × 2 (Q9C944) Histone H2B.1 × 2 (Q9LQQ4) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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 1–103; UniProt 1–103 Author chain F; PDBConstruct 1–103; UniProt 1–103

Probable histone H2A variant 3

Arabidopsis thaliana

UniProt Q9C944

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 1–134 Chain G; UniProt 1–134 Not recorded Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) Histone H2B.1 × 2 (Q9LQQ4) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2AV3_ARATH
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–134; UniProt 1–134 Author chain G; PDBConstruct 1–134; UniProt 1–134

Histone H2B.1

Arabidopsis thaliana

UniProt Q9LQQ4

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 1–148 Chain H; UniProt 1–148 Not recorded Histone H3.1 × 2 (P59226) Histone H4 × 2 (P59259) Probable histone H2A variant 3 × 2 (Q9C944) Widom 601 DNA (147-MER) × 1 Widom 601 DNA (147-MER) × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.87 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.

13 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H2B1_ARATH
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–148; UniProt 1–148 Author chain H; PDBConstruct 1–148; UniProt 1–148

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 9k43

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9k43
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9k43
Deposition date deposition_date2024-10-21
Structure title titleCryo-EM structure of Arabidopsis thaliana H2A.Z-nucleosome with 147bp Widom 601 DNA (C2 symmetry)
Keywords keywordsnucleosome, histone, H2A.Z, Arabidopsis, NUCLEAR PROTEIN/DNA, NUCLEAR PROTEIN-DNA complex; NUCLEAR PROTEIN/DNA
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.10
Radius of gyration Rg (electron density) rg_electron37.34
Forward intensity I(0) i0803591000.00
Molecular weight molecular_weight173180.0 kDa
Excluded volume excluded_volume192180 ų
Envelope volume envelope_volume287760 ų
Hydration-shell volume shell_volume62568 ų
Envelope diameter envelope_diameter116.4
Shell Rg shell_rg45.13
Envelope Rg envelope_rg36.67
Shape Rg shape_rg37.18
Total Rg total_rg38.06
Total atoms total_atoms11814
Residues n_residues1034
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 dmax114.3
Rg (real space) rg_real39.91
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real8.0360e+08
I(0) uncertainty (real space) i0_real_error1.2730e+07
Rg (reciprocal space) rg_reciprocal40.10
I(0) (reciprocal space) i0_reciprocal803800000.0000
Solution quality estimate total_estimate0.8750
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.058
Kurtosis Kurtosis kurtosis-0.703
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha50030000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.992; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.411

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)