8qj0

Room-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO

Method: X-RAY DIFFRACTION Dmax: 133.7 Å Quality: GOOD

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

Ribulose bisphosphate carboxylase small subunit, chloroplastic 2

OrganismNot specified

UniProt Q43832

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain S; UniProt 58–180 Chain T; UniProt 58–180 Chain U; UniProt 58–180 Chain V; UniProt 58–180 Not recorded Ribulose bisphosphate carboxylase large chain × 4 (P00875) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;SpRub solution at a concentration of 15 mg/mL (in a buffer of 20 mM HEPES, 5 mM MgCl2, pH 8.0), combined reservoir solution (0.2 M MgCl2x6H2O, 0.1 M Tris pH 7.0, 12% w/v PEG 8000 Resolution 2.30 Å R-free 0.227

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 RBS2_SPIOL
Isoform
PDB entities 1
Chains and sequence ranges Author chain S; PDBConstruct 1–123; UniProt 58–180 Author chain T; PDBConstruct 1–123; UniProt 58–180 Author chain U; PDBConstruct 1–123; UniProt 58–180 Author chain V; PDBConstruct 1–123; UniProt 58–180

Ribulose bisphosphate carboxylase large chain

OrganismNot specified

UniProt P00875

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain L; UniProt 1–475 Chain M; UniProt 1–475 Chain N; UniProt 1–475 Chain O; UniProt 1–475 Non-standard monomer:Yes (specific site not provided by mmCIF) Ribulose bisphosphate carboxylase small subunit, chloroplastic 2 × 4 (Q43832) MG MAGNESIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;SpRub solution at a concentration of 15 mg/mL (in a buffer of 20 mM HEPES, 5 mM MgCl2, pH 8.0), combined reservoir solution (0.2 M MgCl2x6H2O, 0.1 M Tris pH 7.0, 12% w/v PEG 8000 Resolution 2.30 Å R-free 0.227

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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBL_SPIOL
Isoform
PDB entities 2
Chains and sequence ranges Author chain L; PDBConstruct 1–475; UniProt 1–475 Author chain M; PDBConstruct 1–475; UniProt 1–475 Author chain N; PDBConstruct 1–475; UniProt 1–475 Author chain O; PDBConstruct 1–475; UniProt 1–475

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 8qj0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qj0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qj0
Deposition date deposition_date2023-09-12
Structure title titleRoom-temperature Serial Synchrotron Crystallography structure of Spinacia oleracea RuBisCO
Keywords keywordsSpinacia oleracea, LYASE; LYASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier42.46
Radius of gyration Rg (electron density) rg_electron42.01
Forward intensity I(0) i0951245000.00
Molecular weight molecular_weight253720.0 kDa
Excluded volume excluded_volume316480 ų
Envelope volume envelope_volume413550 ų
Hydration-shell volume shell_volume77352 ų
Envelope diameter envelope_diameter137.0
Shell Rg shell_rg50.60
Envelope Rg envelope_rg42.22
Shape Rg shape_rg42.01
Total Rg total_rg42.34
Total atoms total_atoms35269
Residues n_residues2244
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 dmax133.7
Rg (real space) rg_real42.26
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real9.5120e+08
I(0) uncertainty (real space) i0_real_error1.5190e+07
Rg (reciprocal space) rg_reciprocal42.46
I(0) (reciprocal space) i0_reciprocal951500000.0000
Solution quality estimate total_estimate0.8948
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary57.8
Skewness Skewness skewness0.111
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha238300000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.895

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)