Crystallization and preliminary X-ray diffraction analysis of the arginine repressor ArgR from Bacillus halodurans

Jina Kang, Young Woo Park, Hyun Ku Yeo, Jae Young Lee

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

The arginine repressor (ArgR) is a transcriptional regulator which regulates genes encoding proteins involved in arginine biosynthesis and the arginine catabolic pathway. ArgR from the alkaliphilic bacterium Bacillus halodurans was cloned and overexpressed in Escherichia coli. ArgR (Bh2777) from B. halodurans is composed of 149 amino-acid residues with a molecular mass of 16836Da. ArgR was crystallized at 296K using 1,2-propanediol as a precipitant. Crystals of N-terminally His-tagged ArgR were obtained by the sitting-drop vapour-diffusion method. Dehydrated crystals showed a dramatic improvement in diffraction quality and diffracted to 2.35Å resolution. The crystals belonged to the cubic space group I23, with unit-cell parameters a = b = c = 104.68Å. The asymmetric unit contained one monomer of ArgR, which generates a trimer by the threefold axis of the space group, giving a crystal volume per mass (V M) of 2.98Å3Da-1 and a solvent content of 56.8%.

Original languageEnglish
Pages (from-to)291-294
Number of pages4
JournalActa Crystallographica Section F:Structural Biology Communications
Volume71
DOIs
StatePublished - 1 Mar 2015

Keywords

  • ArgR
  • dehydration
  • transcriptional regulator

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