Cloning, expression, purification, crystallization and preliminary X‐ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Paul, A.; Mishra, A.; Surolia, A.; Vijayan, M.
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1422
• Page End: 1424
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113031138
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The last enzyme in the arginine‐biosynthesis pathway, argininosuccinate lyase, from <italic>Mycobacterium tuberculosis</italic> 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 <italic>P</italic>2₁2₁2₁. Molecular‐replacement calculations and self‐rotation calculations confirmed the space group and the tetrameric nature of the molecule.</p> </abstract>