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Expression, purification and preliminary X-ray analysis of the C-terminal domain of an arginine repressor protein from Mycobacterium tuberculosis.
- 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]
- Subjects :
- *X-rays
*ARGININE
*MYCOBACTERIUM tuberculosis
*CRYSTALS
*PROTEINS
Subjects
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