Open AccessCloning, expression, purification, crystallization and preliminary X‐ray studies of argininosuccinate lyase (Rv1659) from Mycobacterium tuberculosis
Author(s) -
Paul A.,
Mishra A.,
Surolia A.,
Vijayan M.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113031138
Subject(s) - argininosuccinate lyase , orthorhombic crystal system , argininosuccinate synthase , enzyme , mycobacterium tuberculosis , lyase , crystallization , cloning (programming) , chemistry , protein subunit , stereochemistry , crystallography , biochemistry , microbiology and biotechnology , biosynthesis , arginine , biology , tuberculosis , crystal structure , citrulline , amino acid , arginase , gene , organic chemistry , medicine , pathology , computer science , programming language
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 P 2 1 2 1 2 1 . Molecular‐replacement calculations and self‐rotation calculations confirmed the space group and the tetrameric nature of the molecule.