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 language | English |
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Pages (from-to) | 291-294 |
Number of pages | 4 |
Journal | Acta Crystallographica Section F:Structural Biology Communications |
Volume | 71 |
DOIs | |
State | Published - 1 Mar 2015 |
Keywords
- ArgR
- dehydration
- transcriptional regulator