› 5avg

X-ray diffraction
0.95Å resolution

The 0.95 angstrom structure of thaumatin crystallized in high-strength agarose hydrogel

Released:
DOI: 10.2210/pdb5avg/pdb
PDB entry 5avg coloured by chain, front view.
PDB entry 5avg coloured by chain, side view.
PDB entry 5avg coloured by chain, top view.
Source organism: Thaumatococcus daniellii
Primary publication:
Growth of protein crystals in hydrogels prevents osmotic shock.
Sugiyama S, Maruyama M, Sazaki G, Hirose M, Adachi H, Takano K, Murakami S, Inoue T, Mori Y, Matsumura H
J Am Chem Soc 134 5786-9 (2012)
PMID: 22435400

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thaumatin I Chain: A
Molecule details ›
Chain: A
Length: 206 amino acids
Theoretical weight: 22.16 KDa
Source organism: Thaumatococcus daniellii
UniProt:
  • Canonical: P02883 (Residues: 23-228; Coverage: 97%)
Sequence domains: Thaumatin family
Structure domains: Thaumatin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P41212
Unit cell:
a: 57.839Å b: 57.839Å c: 149.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.128 0.127 0.144

Quick links

Citations

3 review citations

An overview of biological macromolecule crystallization.
Russo Krauss et al. (2013)
2 more

2 mentions without citation

A base measure of precision for protein stability predictors: structural sensitivity.
Caldararu et al. (2021)
1 more