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...

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Bibliographic Details
Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-08, Vol.61 (8), p.782-784
Main Authors: Kefala, Georgia, Perry, L. Jeanne, Weiss, Manfred S.
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - isolation & purification
Carboxy-Lyases - chemistry
Carboxy-Lyases - isolation & purification
Cloning, Molecular
CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
Crystallization Communications
DATA ANALYSIS
diaminopimelate decarboxylase
ESCHERICHIA COLI
Gene Expression
LysA
LYSINE
lysine biosynthesis
Mycobacterium tuberculosis - chemistry
Rv1293
SUBSTRATES
X-RAY DIFFRACTION
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Summary: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.
ISSN:1744-3091
1744-3091
DOI:10.1107/S1744309105022839