Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapB (Rv2773c) from Mycobacterium tuberculosis

Journal Article · Fri Jul 01 00:00:00 EDT 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S174430910501938X· OSTI ID:22356146

Kefala, Georgia; Janowski, Robert; Panjikar, Santosh; Mueller-Dieckmann, Christoph

M. tuberculosis dihydrodipicolinate reductase, the enzyme that catalyzes the second committed step of lysine biosynthesis, has been cloned, expressed, purified and crystallized in three different crystal forms. 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.

• OSTI ID: 22356146
• Journal Information: Acta Crystallographica. Section F, Vol. 61, Issue Pt 7; Other Information: PMCID: PMC1952461; PMID: 16511139; PUBLISHER-ID: pu5092; OAI: oai:pubmedcentral.nih.gov:1952461; Copyright (c) International Union of Crystallography 2005; 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
X-RAY DIFFRACTION