3rto

Acoustically mounted porcine insulin microcrystals yield an X-ray SAD structure

Method: X-RAY DIFFRACTION Dmax: 47.9 Å Quality: GOOD

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

Insulin

OrganismNot specified

UniProt P01315

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 88–108 Chain B; UniProt 25–54 Chain C; UniProt 88–108 Chain D; UniProt 25–54 Fragment:Insulin A chain (UNP residues 88-108) Fragment:Insulin B chain (UNP residues 25-54) ZN ZINC ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:SMALL TUBES;pH 6;Microcrystals are obtained by dissolving 0.025 g protein in 5 mL of crystallizing solution (200 mL 0.02 M HCl, 100 mL 0.20 M sodium citrate, 60 mL acetone, 20 mL water, 20 mL 0.12 M zinc sulfate) at 315K. The solution is then rapidly quenched to 293K by immersing it in a cool water bath. Quenching speed determines the resulting crystal size. 20-micron crystals are obtained by quenching in a 293K water bath, 10-micron crystals by quenching in a 283K water bath, and 5-micron crystals by quenching in ice water. pH 6.0, SMALL TUBES Resolution 1.80 Å R-free 0.223

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.

41 other PDB entries and 126 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INS_PIG
Isoform
PDB entities 1, 2
Chains and sequence ranges Author chain A; PDBConstruct 1–21; UniProt 88–108 Author chain C; PDBConstruct 1–21; UniProt 88–108 Author chain B; PDBConstruct 1–30; UniProt 25–54 Author chain D; PDBConstruct 1–30; UniProt 25–54

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 3rto

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3rto
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3rto
Deposition date deposition_date2011-05-03
Structure title titleAcoustically mounted porcine insulin microcrystals yield an X-ray SAD structure
Keywords keywordsHORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier14.80
Radius of gyration Rg (electron density) rg_electron13.69
Forward intensity I(0) i02954670.00
Molecular weight molecular_weight11694.0 kDa
Excluded volume excluded_volume14415 ų
Envelope volume envelope_volume16239 ų
Hydration-shell volume shell_volume10533 ų
Envelope diameter envelope_diameter45.3
Shell Rg shell_rg18.84
Envelope Rg envelope_rg13.95
Shape Rg shape_rg13.65
Total Rg total_rg14.85
Total atoms total_atoms808
Residues n_residues102
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 dmax47.9
Rg (real space) rg_real14.76
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real2.9550e+06
I(0) uncertainty (real space) i0_real_error2.6110e+04
Rg (reciprocal space) rg_reciprocal14.76
I(0) (reciprocal space) i0_reciprocal2955000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.2
Skewness Skewness skewness0.251
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha317700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)