Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Apr 1;65(Pt 4):410-4. doi: 10.1107/S1744309109008628. Epub 2009 Mar 26.

Abstract

The putative transcriptional regulator protein YvoA (BSU35030) from Bacillus subtilis was cloned and heterologously expressed in Escherichia coli. The protein was purified by immobilized metal-affinity chromatography and size-exclusion chromatography and subsequently crystallized. A complete native data set was collected to 2.50 A resolution. The crystals belonged to the monoclinic space group C2 and preliminary analysis of the diffraction data indicated the presence of approximately 12 molecules per asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus subtilis / chemistry*
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / isolation & purification*
  • Bacterial Proteins / metabolism
  • Chromatography, Gel
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Protein Structure, Tertiary
  • X-Ray Diffraction*

Substances

  • Bacterial Proteins