Cloning, purification, crystallization and preliminary crystallographic analysis of a ribokinase from Staphylococcus aureus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jun 1;65(Pt 6):574-6. doi: 10.1107/S1744309109014833. Epub 2009 May 22.

Abstract

The gene SA239 from Staphylococcus aureus encodes a ribokinase that catalyzes the phosphorylation of D-ribose to produce ribose-5-phosphate. Sa239 was crystallized using the hanging-drop vapour-diffusion method. The crystals diffracted to 2.9 A resolution and belonged to space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 91.8, c = 160.7 A. Preliminary crystallographic analysis revealed that the Matthews coefficient V(M) was 3.01 A(3) Da(-1), indicating the presence of one molecule in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Data Collection
  • Escherichia coli / genetics
  • Genes, Bacterial
  • Phosphotransferases (Alcohol Group Acceptor) / chemistry*
  • Phosphotransferases (Alcohol Group Acceptor) / genetics
  • Phosphotransferases (Alcohol Group Acceptor) / isolation & purification*
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Protein Binding
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / isolation & purification
  • Recombinant Fusion Proteins / metabolism
  • Staphylococcus aureus / enzymology*
  • Statistics as Topic
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • Phosphotransferases (Alcohol Group Acceptor)
  • ribokinase