title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis.
abstract: 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.
authors.affiliation: EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
authors.forename: Georgia
authors.initials: G
authors.lastname: Kefala
authors.forename: L Jeanne
authors.initials: LJ
authors.lastname: Perry
authors.forename: Manfred S
authors.initials: MS
authors.lastname: Weiss
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification*; D002262:Carboxy-Lyases / Q000737:chemistry* / Q000302:isolation & purification*; D003001:Cloning, Molecular; D003460:Crystallization; D015870:Gene Expression; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D001426:Bacterial Proteins; D002262:Carboxy-Lyases; C079912:LysA protein, Bacteria