Open AccessCloning, expression, purification, crystallization and X‐ray crystallographic analysis of Rv2606c from Mycobacterium tuberculosis H37Rv
Author(s) -
Kim Sangwoo,
Kim KyungJin
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113010683
Subject(s) - crystallization , mycobacterium tuberculosis , crystallography , chemistry , glutamine amidotransferase , biosynthesis , pyridoxal , tuberculosis , biology , microbiology and biotechnology , biochemistry , glutamine , gene , medicine , enzyme , amino acid , organic chemistry , pathology
Tuberculosis is a widespread and deadly infectious disease, and one third of the human population is already infected. Vitamin B 6 is known to be synthesized through consecutive reactions mediated by pyridoxal biosynthesis lyase (PdxS) and glutamine amidotransferase (PdxT). The gene product Rv2606c, the PdxS pyridoxal biosynthesis lyase from Mycobacterium tuberculosis , was crystallized using the hanging‐drop vapour‐diffusion method in the presence of 8%( w / v ) PEG 8000, 0.1 M 3‐(cyclohexylamino)‐1‐propanesulfonic acid pH 10.5 and 0.2 M sodium chloride at 295 K. X‐ray diffraction data were collected to a maximum resolution of 1.7 Å on a synchrotron beamline. The crystal belonged to space group I 222 or I 2 1 2 1 2 1 , with unit‐cell parameters a = 110.75, b = 126.08, c = 180.82 Å, α = β = γ = 90°. With three molecules per asymmetric unit, the crystal volume per unit protein weight ( V M ) was 3.79 Å 3 Da −1 .