Akif, M. and Chauhan, R. and Mande, S.C. (2004) Expression, purification, crystallization and preliminary X-ray crystallographic studies of Mycobacterium tuberculosisthioredoxin reductase. Acta Crystallographica Section D Biological Crystallography, 60 (4). pp. 777-779. ISSN 0907-4449

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Abstract

Mycobacterium tuberculosis (H37Rv), the causative agent of the dreaded disease tuberculosis, contains three thioredoxins and a single thioredoxin reductase. Thioredoxin reductase is a member of the pyridine-nucleotide disulfide oxidoreductase family of flavoenzymes. The thioredoxin reductase gene with a His tag at the C-terminus was expressed in Escherichia coli and purified. The dimeric (70 kDa) protein was incubated with 10 mM DTT for 30 min and then crystallized using the hanging-drop vapour-diffusion method in the presence of 15% PEG 3350 and phosphate-citrate buffer pH 5 at room temperature (298 K). A diffraction data set complete to 3 A resolution has been collected under cryoconditions and the space group was determined to be P4(1)2(1)2, with unit-cell parameters a = 107.4, c = 118.2 A. Matthews coefficient calculations revealed the presence of two monomers in the asymmetric unit.

Item Type:	Article
Depositing User:	Users 2 not found.
Date Deposited:	13 Oct 2015 10:37
Last Modified:	13 Oct 2015 10:37
URI:	http://cdfd.sciencecentral.in/id/eprint/545

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