Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis.
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.
Kefala
Georgia
G
EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg, Germany.
Perry
L Jeanne
LJ
Weiss
Manfred S
MS
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
D001426:Bacterial Proteins; D002262:Carboxy-Lyases; C079912:LysA protein, Bacteria