Open AccessCloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of DapC (Rv0858c) from Mycobacterium tuberculosis
Author(s) -
Weyand Simone,
Kefala Georgia,
Weiss Manfred S.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106026753
Subject(s) - tetragonal crystal system , orthorhombic crystal system , mycobacterium tuberculosis , escherichia coli , crystallization , dimer , crystallography , cloning (programming) , monomer , crystal (programming language) , chemistry , crystal structure , tuberculosis , biochemistry , gene , polymer , organic chemistry , medicine , pathology , computer science , programming language
N ‐Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis (DAP‐AT; DapC; Rv0858c) has been cloned, heterologously expressed in Escherichia coli , purified using standard chromatographic techniques and crystallized in two related crystal forms. Preliminary diffraction data analysis suggests the presence of a monomer in the asymmetric unit of the tetragonal crystal form and a dimer in the asymmetric unit of the orthorhombic crystal form.