Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the L,D‐transpeptidase Ldt Mt1 from Mycobacterium tuberculosis

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the... Mycobacterium tuberculosis is capable of adapting to prolonged periods of dormancy, a state which is resistant to killing by antimycobacterial agents. The L,D‐transpeptidation reaction catalysed by the L,D‐transpeptidase LdtMt1 is likely to play an essential role in the adaptation of M. tuberculosis to its dormant state. LdtMt1 has been successfully crystallized using vapour‐diffusion methods. The crystals of this protein belonged to space group P6522, with unit‐cell parameters a = 57.25, b = 57.25, c = 257.96 Å, α = 90, β = 90, γ = 120°. Diffraction data have also been collected from a selenomethionine derivative to 2.9 Å resolution. Model building using the phases derived from the multiwavelength anomalous dispersion experiment is in progress. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Expression, purification, crystallization and preliminary X‐ray crystallographic analysis of the L,D‐transpeptidase Ldt Mt1 from Mycobacterium tuberculosis

Loading next page...
 
/lp/wiley/expression-purification-crystallization-and-preliminary-x-ray-kfexTHolIv

References (34)

Publisher
Wiley
Copyright
International Union of Crystallography, 2013
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309112052141
pmid
23519798
Publisher site
See Article on Publisher Site

Abstract

Mycobacterium tuberculosis is capable of adapting to prolonged periods of dormancy, a state which is resistant to killing by antimycobacterial agents. The L,D‐transpeptidation reaction catalysed by the L,D‐transpeptidase LdtMt1 is likely to play an essential role in the adaptation of M. tuberculosis to its dormant state. LdtMt1 has been successfully crystallized using vapour‐diffusion methods. The crystals of this protein belonged to space group P6522, with unit‐cell parameters a = 57.25, b = 57.25, c = 257.96 Å, α = 90, β = 90, γ = 120°. Diffraction data have also been collected from a selenomethionine derivative to 2.9 Å resolution. Model building using the phases derived from the multiwavelength anomalous dispersion experiment is in progress.

Journal

Acta Crystallographica Section FWiley

Published: Mar 1, 2013

There are no references for this article.