Skip to main navigation Skip to search Skip to main content

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

  • Jiansong Ju
  • , Jianxun Qi
  • , Shujing Xu
  • , Kouhei Ohnishi
  • , Michael J. Benedik
  • , Yanfen Xue
  • , Yanhe Ma*
  • *Corresponding author for this work
  • CAS - Institute of Microbiology
  • CAS - Institute of Physics
  • Shaanxi University of Science and Technology
  • Kochi University
  • Texas A&M University

Research output: Contribution to journalArticlepeer-review

Abstract

Alanine racemase (DadXOF4), a dimeric endogenous PLP-dependent alkaline enzyme from alkaliphilic Bacillus pseudofirmus OF4, was expressed in Escherichia coli and purified with a His6 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 P212121, with two protein molecules in the asymmetric unit.

Original languageEnglish
Pages (from-to)166-168
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number2
DOIs
Publication statusPublished - 2009
Externally publishedYes

Keywords

  • Alkaline alanine racemase
  • Bacillus pseudofirmus OF4

Fingerprint

Dive into the research topics of 'Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4'. Together they form a unique fingerprint.

Cite this