Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jun 1;64(Pt 6):520-3. doi: 10.1107/S1744309108012244. Epub 2008 May 23.

Abstract

Biotin protein ligase from Staphylococcus aureus catalyses the biotinylation of acetyl-CoA carboxylase and pyruvate carboxylase. Recombinant biotin protein ligase from S. aureus has been cloned, expressed and purified. Crystals were grown using the hanging-drop vapour-diffusion method using PEG 8000 as the precipitant at 295 K. X-ray diffraction data were collected to 2.3 A resolution from crystals using synchrotron X-ray radiation at 100 K. The diffraction was consistent with the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 93.665, c = 131.95.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification*
  • Biotin / chemistry*
  • Biotin / genetics
  • Biotinylation
  • Carbon-Nitrogen Ligases / chemistry*
  • Carbon-Nitrogen Ligases / genetics
  • Carbon-Nitrogen Ligases / isolation & purification*
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli / genetics
  • Histidine / chemistry
  • Molecular Weight
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Staphylococcus aureus / enzymology*
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Histidine
  • Biotin
  • Carbon-Nitrogen Ligases