8xg5

X-ray crystal structure of streptavidin flash-cooled in 30% PEG1000 at ambient pressure

Method: X-RAY DIFFRACTION Dmax: 68.1 Å Quality: EXCELLENT

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

Streptavidin

OrganismNot specified

UniProt P22629

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 39–159 Chain D; UniProt 39–159 Fragment:Avidin-like PG4 TETRAETHYLENE GLYCOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M MES pH 6.0, 20% PEG 1000 Resolution 1.40 Å R-free 0.183
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 39–159 Chain C; UniProt 39–159 Fragment:Avidin-like PG4 TETRAETHYLENE GLYCOL × 1 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M MES pH 6.0, 20% PEG 1000 Resolution 1.40 Å R-free 0.183

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.

312 other PDB entries and 367 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAV_STRAV
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–121; UniProt 39–159 Author chain B; PDBConstruct 1–121; UniProt 39–159 Author chain C; PDBConstruct 1–121; UniProt 39–159 Author chain D; PDBConstruct 1–121; UniProt 39–159

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 8xg5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8xg5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8xg5
Deposition date deposition_date2023-12-15
最后修订 last_revision2024-12-18
Structure title titleX-ray crystal structure of streptavidin flash-cooled in 30% PEG1000 at ambient pressure
Keywords keywordsstreptavidin, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.71
Radius of gyration Rg (electron density) rg_electron21.61
Forward intensity I(0) i045051200.00
Molecular weight molecular_weight50331.0 kDa
Excluded volume excluded_volume62153 ų
Envelope volume envelope_volume73125 ų
Hydration-shell volume shell_volume27163 ų
Envelope diameter envelope_diameter68.2
Shell Rg shell_rg29.08
Envelope Rg envelope_rg21.84
Shape Rg shape_rg21.58
Total Rg total_rg22.55
Total atoms total_atoms3565
Residues n_residues469
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 dmax68.1
Rg (real space) rg_real22.56
Rg uncertainty (real space) rg_real_error0.26
I(0) (real space) i0_real4.5050e+07
I(0) uncertainty (real space) i0_real_error5.2660e+05
Rg (reciprocal space) rg_reciprocal22.59
I(0) (reciprocal space) i0_reciprocal45050000.0000
Solution quality estimate total_estimate0.9086
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-0.542
Angular range angular_range— – 0.3500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10610000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.946; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)