Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapA (Rv2753c) from Mycobacterium tuberculosis

Journal Article · Wed Nov 01 00:00:00 EST 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106039844· OSTI ID:22356394

Kefala, Georgia

M. tuberculosis dihydrodipicolinate synthase, the enzyme that catalyzes the first unique reaction in the l-lysine biosynthesis pathway, has been cloned, expressed, purified and crystallized and the crystals have been characterized by X-ray diffraction. Dihydrodipicolinate synthase from Mycobacterium tuberculosis (DHDPS, DapA, Rv2753c) has been cloned, heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in a monoclinic crystal form. Preliminary diffraction data analysis suggests the presence of two independent tetramers in the asymmetric unit in almost the same relative orientation.

• OSTI ID: 22356394
• Journal Information: Acta Crystallographica. Section F, Vol. 62, Issue Pt 11; Other Information: PMCID: PMC2225217; PMID: 17077492; PUBLISHER-ID: hc5013; OAI: oai:pubmedcentral.nih.gov:2225217; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTALLIZATION
CRYSTALS
DATA ANALYSIS
ESCHERICHIA COLI
LYSINE
ORIENTATION
X-RAY DIFFRACTION