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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1422-4. doi: 10.1107/S1744309113031138. Epub 2013 Nov 29.

Cloning, expression, purification, crystallization and preliminary X-ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis.

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1
Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.

Abstract

The last enzyme in the arginine-biosynthesis pathway, argininosuccinate lyase, from Mycobacterium tuberculosis has been cloned, expressed, purified and crystallized, and preliminary X-ray studies have been carried out on the crystals. The His-tagged tetrameric enzyme with a subunit molecular weight of 50.9 kDa crystallized with two tetramers in the asymmetric unit of the orthorhombic unit cell, space group P2(1)2(1)2(1). Molecular-replacement calculations and self-rotation calculations confirmed the space group and the tetrameric nature of the molecule.

KEYWORDS:

Mycobacterium tuberculosis; Rv1659; argininosuccinate lyase

PMID:
24316845
PMCID:
PMC3855735
DOI:
10.1107/S1744309113031138
[Indexed for MEDLINE]
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