Published July 30, 2005 | Version v1
Journal article

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of LysA (Rv1293) from Mycobacterium tuberculosis

  • 1. EMBL Hamburg Outstation, c/o DESY, Notkestrasse 85, D-22603 Hamburg (Germany)
  • 2. UCLA-DOE Laboratory of Structural Biology and Molecular Medicine, 206 Boyer Hall, Box 951570, Los Angeles, CA 90095-1570 (United States)

Description

M. tuberculosis diaminopimelate decarboxylase, the enzyme that catalyzes the final step of lysine biosynthesis, has been cloned, expressed, purified and crystallized in the absence of cofactor or substrate. 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

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309105022839; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952341

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
61
Journal Issue
Pt 8
Journal Page Range
p. 782-784
ISSN
1744-3091
CODEN
ACSFCL

INIS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2005
Notes
PMCID: PMC1952341; PMID: 16511157; PUBLISHER-ID: vr5048; OAI: oai:pubmedcentral.nih.gov:1952341