Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):166-8. doi: 10.1107/S174430910900013X. Epub 2009 Jan 31.

Abstract

Alanine racemase (DadX(OF4)), a dimeric endogenous PLP-dependent alkaline enzyme from alkaliphilic Bacillus pseudofirmus OF4, was expressed in Escherichia coli and purified with a His(6) tag in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop vapour-diffusion method at 291 K using a solution containing 1.4 M sodium/potassium phosphate pH 8.2. The protein crystallized in space group P2(1)2(1)2(1), with two protein molecules in the asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alanine Racemase / chemistry*
  • Alanine Racemase / isolation & purification
  • Bacillus / enzymology*
  • Crystallization
  • Crystallography, X-Ray*
  • Hydrogen-Ion Concentration

Substances

  • Alanine Racemase