Open AccessExpression, purification, crystallization and preliminary X‐ray analysis of two arginine‐biosynthetic enzymes from Mycobacterium tuberculosis
Author(s) -
Moradian Fatemeh,
Garen Craig,
Cherney Leonid,
Cherney Maia,
James Michael N. G.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106034609
Subject(s) - escherichia coli , mycobacterium tuberculosis , ornithine carbamoyltransferase , enzyme , reductase , arginine , biochemistry , microbiology and biotechnology , biosynthesis , gene , biology , open reading frame , chemistry , ornithine , tuberculosis , amino acid , peptide sequence , medicine , pathology
The gene products of two open reading frames from Mycobacterium tuberculosis ( Mtb ) have been crystallized using the sitting‐drop vapour‐diffusion method. Rv1652 encodes a putative N ‐acetyl‐γ‐glutamyl‐phosphate reductase ( Mtb AGPR), while the Rv1656 gene product is annotated as ornithine carbamoyltransferase ( Mtb OTC). Both Mtb AGPR and Mtb OTC were expressed in Escherichia coli , purified to homogeneity and crystallized. Native data for each crystal were collected to resolutions of 2.15 and 2.80 Å, respectively. Preliminary X‐ray data are presented for both enzymes.