7o7u

Crystal structure of rsEGFP2 in the non-fluorescent off-state determined by serial femtosecond crystallography at room temperature

Method: X-RAY DIFFRACTION Dmax: 61.5 Å Quality: GOOD

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

Green fluorescent protein

Aequorea victoria

UniProt P42212

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–238 Mutation:M1_S2insV, F64L, S65T, H231L, A206K, Q69L, V163S, T65A Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:BATCH MODE;pH 8;293 K;100 mM HEPES pH 8.0, 2 M ammonium sulphate Resolution 1.70 Å R-free 0.215

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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 14–250; UniProt 1–238

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 7o7u

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7o7u
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7o7u
Deposition date deposition_date2021-04-13
Structure title titleCrystal structure of rsEGFP2 in the non-fluorescent off-state determined by serial femtosecond crystallography at room temperature
Keywords keywordsReversibly photoswitchable fluorescent protein, FLUORESCENT PROTEIN; FLUORESCENT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.99
Radius of gyration Rg (electron density) rg_electron17.70
Forward intensity I(0) i013115500.00
Molecular weight molecular_weight26980.0 kDa
Excluded volume excluded_volume33723 ų
Envelope volume envelope_volume38863 ų
Hydration-shell volume shell_volume18312 ų
Envelope diameter envelope_diameter62.6
Shell Rg shell_rg24.04
Envelope Rg envelope_rg18.09
Shape Rg shape_rg17.68
Total Rg total_rg18.71
Total atoms total_atoms1905
Residues n_residues237
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 dmax61.5
Rg (real space) rg_real18.92
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real1.3120e+07
I(0) uncertainty (real space) i0_real_error1.8320e+05
Rg (reciprocal space) rg_reciprocal18.93
I(0) (reciprocal space) i0_reciprocal13120000.0000
Solution quality estimate total_estimate0.8058
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.9
Skewness Skewness skewness0.283
Kurtosis Kurtosis kurtosis-0.272
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4120000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)