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

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

Acta Crystallogr Sect F Struct Biol Cryst Commun

Protein Structure and Function Group, Department of Biochemistry, The University of Alberta, Edmonton, Alberta T6G 2H7, Canada.

Published: November 2007

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.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2339742PMC
http://dx.doi.org/10.1107/S1744309107046374DOI Listing

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