Literature DB >> 24316845

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

A Paul1, A Mishra, A Surolia, M Vijayan.   

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.

Entities:  

Keywords:  Mycobacterium tuberculosis; Rv1659; argininosuccinate lyase

Mesh:

Substances:

Year:  2013        PMID: 24316845      PMCID: PMC3855735          DOI: 10.1107/S1744309113031138

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  24 in total

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