8wpz

Cryo-ET structure of RuBisCO at 3.9 angstroms from Synechococcus elongatus PCC 7942

Method: ELECTRON MICROSCOPY Dmax: 144.7 Å Quality: GOOD

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

Ribulose bisphosphate carboxylase small subunit

OrganismNot specified

UniProt Q31NB2

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 heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain A; UniProt 1–111 Chain B; UniProt 1–111 Chain E; UniProt 1–111 Chain F; UniProt 1–111 Chain I; UniProt 1–111 Chain L; UniProt 1–111 Chain M; UniProt 1–111 Chain P; UniProt 1–111 Not recorded Ribulose bisphosphate carboxylase large chain × 8 (Q31NB3) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

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

View Construct and Data Evidence
UniProt name RBS_SYNE7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–111; UniProt 1–111 Author chain B; PDBConstruct 1–111; UniProt 1–111 Author chain E; PDBConstruct 1–111; UniProt 1–111 Author chain F; PDBConstruct 1–111; UniProt 1–111 Author chain I; PDBConstruct 1–111; UniProt 1–111 Author chain L; PDBConstruct 1–111; UniProt 1–111 Author chain M; PDBConstruct 1–111; UniProt 1–111 Author chain P; PDBConstruct 1–111; UniProt 1–111

Ribulose bisphosphate carboxylase large chain

OrganismNot specified

UniProt Q31NB3

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 heterocomplex Heteromer Protein × 16 PDB declaration: hexadecameric(16) Consistent with protein copy count Chain C; UniProt 1–472 Chain D; UniProt 1–472 Chain G; UniProt 1–472 Chain H; UniProt 1–472 Chain J; UniProt 1–472 Chain K; UniProt 1–472 Chain N; UniProt 1–472 Chain O; UniProt 1–472 Not recorded Ribulose bisphosphate carboxylase small subunit × 8 (Q31NB2) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.90 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBL_SYNE7
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–472; UniProt 1–472 Author chain D; PDBConstruct 1–472; UniProt 1–472 Author chain G; PDBConstruct 1–472; UniProt 1–472 Author chain H; PDBConstruct 1–472; UniProt 1–472 Author chain J; PDBConstruct 1–472; UniProt 1–472 Author chain K; PDBConstruct 1–472; UniProt 1–472 Author chain N; PDBConstruct 1–472; UniProt 1–472 Author chain O; PDBConstruct 1–472; UniProt 1–472

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 8wpz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8wpz
Deposition date deposition_date2023-10-10
Structure title titleCryo-ET structure of RuBisCO at 3.9 angstroms from Synechococcus elongatus PCC 7942
Keywords keywordscarboxysome, RuBisCO, cryo-et, PHOTOSYNTHESIS; PHOTOSYNTHESIS
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.12
Radius of gyration Rg (electron density) rg_electron48.13
Forward intensity I(0) i03649220000.00
Molecular weight molecular_weight507150.0 kDa
Excluded volume excluded_volume633570 ų
Envelope volume envelope_volume848060 ų
Hydration-shell volume shell_volume133050 ų
Envelope diameter envelope_diameter145.3
Shell Rg shell_rg61.53
Envelope Rg envelope_rg47.54
Shape Rg shape_rg48.16
Total Rg total_rg48.40
Total atoms total_atoms35774
Residues n_residues4492
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 dmax144.7
Rg (real space) rg_real48.57
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real3.6490e+09
I(0) uncertainty (real space) i0_real_error5.9760e+07
Rg (reciprocal space) rg_reciprocal49.11
I(0) (reciprocal space) i0_reciprocal3652000000.0000
Solution quality estimate total_estimate0.8830
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary67.8
Skewness Skewness skewness-0.036
Kurtosis Kurtosis kurtosis-0.576
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1720000000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.936; Smooth: 0.789

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)