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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification*
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Carboxy-Lyases / chemistry*
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Carboxy-Lyases / isolation & purification*
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Cloning, Molecular
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Crystallization
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Gene Expression*
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Mycobacterium tuberculosis / chemistry*
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X-Ray Diffraction
Substances
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Bacterial Proteins
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Carboxy-Lyases
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LysA protein, Bacteria