8ba7

CryoEM structure of nucleotide-free GroEL-Rubisco.

Method: ELECTRON MICROSCOPY Dmax: 171.9 Å Quality: REASONABLE

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

Chaperonin GroEL

Escherichia coli

UniProt P0A6F5

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 homooligomer Homooligomer Protein × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 2–548 Chain B; UniProt 2–548 Chain C; UniProt 2–548 Chain D; UniProt 2–548 Chain E; UniProt 2–548 Chain F; UniProt 2–548 Chain G; UniProt 2–548 Chain H; UniProt 2–548 Chain I; UniProt 2–548 Chain J; UniProt 2–548 Chain K; UniProt 2–548 Chain L; UniProt 2–548 Chain M; UniProt 2–548 Chain N; UniProt 2–548 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;The grid was prepared using a chameleon (SPT Labtech). Resolution 4.40 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.

81 other PDB entries and 95 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CH60_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–547; UniProt 2–548 Author chain B; PDBConstruct 1–547; UniProt 2–548 Author chain C; PDBConstruct 1–547; UniProt 2–548 Author chain D; PDBConstruct 1–547; UniProt 2–548 Author chain E; PDBConstruct 1–547; UniProt 2–548 Author chain F; PDBConstruct 1–547; UniProt 2–548 Author chain G; PDBConstruct 1–547; UniProt 2–548 Author chain H; PDBConstruct 1–547; UniProt 2–548 Author chain I; PDBConstruct 1–547; UniProt 2–548 Author chain J; PDBConstruct 1–547; UniProt 2–548 Author chain K; PDBConstruct 1–547; UniProt 2–548 Author chain L; PDBConstruct 1–547; UniProt 2–548 Author chain M; PDBConstruct 1–547; UniProt 2–548 Author chain N; PDBConstruct 1–547; UniProt 2–548

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 8ba7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ba7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ba7
Deposition date deposition_date2022-10-11
Structure title titleCryoEM structure of nucleotide-free GroEL-Rubisco.
Keywords keywordsGroEL, Rubisco, Chaperone, complex; CHAPERONE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.21
Radius of gyration Rg (electron density) rg_electron64.04
Forward intensity I(0) i08399070000.00
Molecular weight molecular_weight771730.0 kDa
Excluded volume excluded_volume966860 ų
Envelope volume envelope_volume1590200 ų
Hydration-shell volume shell_volume197550 ų
Envelope diameter envelope_diameter190.8
Shell Rg shell_rg75.51
Envelope Rg envelope_rg60.02
Shape Rg shape_rg64.07
Total Rg total_rg64.15
Total atoms total_atoms109676
Residues n_residues7336
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 dmax171.9
Rg (real space) rg_real64.45
Rg uncertainty (real space) rg_real_error0.72
I(0) (real space) i0_real8.3990e+09
I(0) uncertainty (real space) i0_real_error1.5710e+08
Rg (reciprocal space) rg_reciprocal65.83
I(0) (reciprocal space) i0_reciprocal8419000000.0000
Solution quality estimate total_estimate0.6102
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary93.1
Skewness Skewness skewness-0.101
Kurtosis Kurtosis kurtosis-0.541
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4018000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.972; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.975; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)