Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis
Author(s) -
Kefala Georgia,
Perry L. Jeanne,
Weiss Manfred S.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105022839
Subject(s) - homotetramer , mycobacterium tuberculosis , cloning (programming) , escherichia coli , crystallization , chemistry , tuberculosis , microbiology and biotechnology , biology , biochemistry , organic chemistry , medicine , gene , pathology , protein subunit , computer science , programming language
Diaminopimelate decarboxylase from Mycobacterium tuberculosis (LysA, DAPDC, Rv1293) has been cloned and heterologously expressed in Escherichia coli , purified using standard chromatographic techniques and crystallized. Preliminary diffraction data analysis suggests the presence of a homotetramer in the asymmetric unit.