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

被引:5
|
作者
Lu, George J. [1 ]
Garen, Craig R. [1 ]
Cherney, Maia M. [1 ]
Cherney, Leonid T. [1 ]
Lee, Cecilia [1 ]
James, Michael N. G. [1 ]
机构
[1] Univ Alberta, Dept Biochem, Protein Struct & Funct Grp, Edmonton, AB T6G 2H7, Canada
关键词
D O I
10.1107/S1744309107046374
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 angstrom. 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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收藏
页码:936 / 939
页数:4
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