Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of DapC (Rv0858c) from Mycobacterium tuberculosis

Journal Article · Tue Aug 01 00:00:00 EDT 2006 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309106026753· OSTI ID:22360179

Weyand, Simone; Kefala, Georgia

M. tuberculosis N-succinyldiaminopimelate aminotransferase, the enzyme which catalyzes the sixth reaction in the lysine-biosynthesis pathway, has been cloned, expressed, purified and crystallized. N-Succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis (DAP-AT; DapC; Rv0858c) has been cloned, heterologously expressed in Escherichia coli, purified using standard chromatographic techniques and crystallized in two related crystal forms. Preliminary diffraction data analysis suggests the presence of a monomer in the asymmetric unit of the tetragonal crystal form and a dimer in the asymmetric unit of the orthorhombic crystal form.

• OSTI ID: 22360179
• Journal Information: Acta Crystallographica. Section F, Vol. 62, Issue Pt 8; Other Information: PMCID: PMC2242922; PMID: 16880560; PUBLISHER-ID: fw5099; OAI: oai:pubmedcentral.nih.gov:2242922; 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
DIMERS
ESCHERICHIA COLI
LYSINE
MONOMERS
X-RAY DIFFRACTION