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

Expression, purification and preliminary X‐ray analysis of the C‐terminal domain of an arginine... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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References (14)

Publisher
Wiley
Copyright
Copyright © 2007 Wiley Subscription Services, Inc., A Wiley Company
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309107046374
pmid
18007044
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Nov 1, 2007

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