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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis
DOI: 10.1107/S1744309105022839
Additional Information
How to Cite
Kefala, G., Perry, L. J. and Weiss, M. S. (2005), Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis. Acta Crystallographica Section F, 61: 782–784. doi: 10.1107/S1744309105022839
Keywords:
- diaminopimelate decarboxylase;
- LysA;
- Rv1293;
- lysine biosynthesis.
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.