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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis
DOI: 10.1107/S174430910501938X
Additional Information
How to Cite
Kefala, G., Janowski, R., Panjikar, S., Mueller-Dieckmann, C. and Weiss, M. S. (2005), Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis. Acta Crystallographica Section F, 61: 718–721. doi: 10.1107/S174430910501938X
Keywords:
- dihydrodipicolinate reductase;
- lysine biosynthesis.
Dihydrodipicolinate reductase from Mycobacterium tuberculosis (DapB, DHDPR, Rv2773c) has been cloned and heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in three different crystal forms. Preliminary diffraction data analysis suggests the presence of two tetramers in the asymmetric unit of one crystal form and half a tetramer in the other two crystal forms.