Back to Search Start Over

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

Authors :
Lu, George J.
Garen, Craig R.
Cherney, Maia M.
Cherney, Leonid T.
Lee, Cecilia
James, Michael N. G.
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Nov2007, Vol. 63 Issue 11, p936-939. 4p. 1 Color Photograph, 1 Black and White Photograph, 2 Diagrams, 1 Chart.
Publication Year :
2007

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 Å. 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
63
Issue :
11
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
27608313
Full Text :
https://doi.org/10.1107/S1744309107046374