› 1bxy

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.

Released:
DOI: 10.2210/pdb1bxy/pdb
PDB entry 1bxy coloured by chain, front view.
PDB entry 1bxy coloured by chain, side view.
PDB entry 1bxy coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 A resolution: conformational flexibility of the molecule.
Fedorov R, Nevskaya N, Khairullina A, Tishchenko S, Mikhailov A, Garber M, Nikonov S
Acta Crystallogr D Biol Crystallogr 55 1827-33 (1999)
PMID: 10531479

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Large ribosomal subunit protein uL30 Chains: A, B
Molecule details ›
Chains: A, B
Length: 60 amino acids
Theoretical weight: 6.8 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P74909 (Residues: 1-60; Coverage: 100%)
Gene names: rpl30, rpmD
Sequence domains: Ribosomal protein L30p/L7e
Structure domains: Ribosomal protein L30, ferredoxin-like fold domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P3221
Unit cell:
a: 63.5Å b: 63.5Å c: 77.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.203 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

High resolution structure of the large ribosomal subunit from a mesophilic eubacterium.
Harms et al. (2001)
2 more

5 mentions without citation

Calculation of accurate small angle X-ray scattering curves from coarse-grained protein models.
Stovgaard et al. (2010)
4 more