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Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis.

ABSTRACT: 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 A. The crystals belong to space group P1 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.

SUBMITTER: Lu GJ

PROVIDER: S-EPMC2339742 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature

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Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis.

Lu George J GJ Garen Craig R CR Cherney Maia M MM Cherney Leonid T LT Lee Cecilia C James Michael N G MN

Acta crystallographica. Section F, Structural biology and crystallization communications 20071024 Pt 11

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 A. The crystals belong to space group P1 and the Matthews coefficient suggests that the ...[more]

PMID: 18007044

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