Open AccessExpression, purification and preliminary X‐ray analysis of the C‐terminal domain of an arginine repressor protein from Mycobacterium tuberculosis
Author(s) -
Lu George J.,
Garen Craig R.,
Cherney Maia M.,
Cherney Leonid T.,
Lee Cecilia,
James Michael N. G.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107046374
Subject(s) - repressor , arginine , mycobacterium tuberculosis , open reading frame , chemistry , biochemistry , microbiology and biotechnology , biology , gene , gene expression , peptide sequence , tuberculosis , amino acid , medicine , pathology
The gene product of an open reading frame Rv1657 from Mycobacterium tuberculosis is a putative arginine repressor protein (ArgR), a transcriptional factor that regulates the expression of arginine‐biosynthetic enzymes. Rv1657 was expressed and purified and a C‐terminal domain was crystallized using the hanging‐drop vapour‐diffusion method. Diffraction data were collected and processed to a resolution of 2.15 Å. The crystals belong to space group P 1 and the Matthews coefficient suggests that the crystals contain six C‐terminal domain molecules per unit cell. Previous structural and biochemical studies on the arginine repressor proteins from other organisms have likewise shown the presence of six molecules per unit cell.