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

Learn More →

Purification, crystallization and diffraction studies of the methyltransferases BT_2972 and BVU_3255 from antibiotic‐resistant pathogens of the genus Bacteroides from the human intestine

Purification, crystallization and diffraction studies of the methyltransferases BT_2972 and... The methyltransferases BT_2972 and BVU_3255 from two different Bacteroides species that are antibiotic‐resistant pathogens from the human intestine were cloned, overexpressed and purified, yielding approximately 120 mg of each protein from 1 l culture. Apo BT_2972 and BVU_3255 and their complexes with S‐adenosylmethionine or S‐adenosylhomocysteine were crystallized in four different crystal forms using the hanging‐drop vapour‐diffusion method. These crystals diffracted to resolutions ranging from 2.8 to 2.2 Å. Sequence analysis suggested that the two proteins are homologous small‐molecule methyltransferases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Purification, crystallization and diffraction studies of the methyltransferases BT_2972 and BVU_3255 from antibiotic‐resistant pathogens of the genus Bacteroides from the human intestine

Loading next page...
 
/lp/wiley/purification-crystallization-and-diffraction-studies-of-the-YHicd20dmZ

References (16)

Publisher
Wiley
Copyright
International Union of Crystallography, 2011
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111031812
pmid
22102231
Publisher site
See Article on Publisher Site

Abstract

The methyltransferases BT_2972 and BVU_3255 from two different Bacteroides species that are antibiotic‐resistant pathogens from the human intestine were cloned, overexpressed and purified, yielding approximately 120 mg of each protein from 1 l culture. Apo BT_2972 and BVU_3255 and their complexes with S‐adenosylmethionine or S‐adenosylhomocysteine were crystallized in four different crystal forms using the hanging‐drop vapour‐diffusion method. These crystals diffracted to resolutions ranging from 2.8 to 2.2 Å. Sequence analysis suggested that the two proteins are homologous small‐molecule methyltransferases.

Journal

Acta Crystallographica Section FWiley

Published: Nov 1, 2011

There are no references for this article.