6wa8

X-ray diffraction
3.3Å resolution

Crystal structure of the E. coli transcription termination factor Rho

Released:
Source organism: Escherichia coli K-12
Primary publication:
Crystal structure of the Escherichia coli transcription termination factor Rho.
Acta Crystallogr F Struct Biol Commun 76 398-405 (2020)
PMID: 32880587

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription termination factor Rho Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 419 amino acids
Theoretical weight: 47.07 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AG30 (Residues: 1-419; Coverage: 100%)
Gene names: JW3756, b3783, nitA, psuA, rho, rnsC, sbaA, tsu
Sequence domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: C2
Unit cell:
a: 161.745Å b: 101.902Å c: 184.016Å
α: 90° β: 107.77° γ: 90°
R-values:
R R work R free
0.254 0.252 0.296
Expression system: Escherichia coli BL21(DE3)