Please use this identifier to cite or link to this item: https://doi.org/10.1107/S1744309111031812
Title: 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
Authors: Kumar, V.
Mallika, N.
Sivaraman, J. 
Keywords: antibiotic resistance
Bacteroides thetaiotaomicron
Bacteroides vulgatus
BT-2972
BVU-3255
S-adenosylhomocysteine
S-adenosylmethionine
small-molecule methyltransferases
Issue Date: Nov-2011
Citation: Kumar, V., Mallika, N., Sivaraman, J. (2011-11). 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. Acta Crystallographica Section F: Structural Biology and Crystallization Communications 67 (11) : 1359-1362. ScholarBank@NUS Repository. https://doi.org/10.1107/S1744309111031812
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. © 2011 International Union of Crystallography. All rights reserved.
Source Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications
URI: http://scholarbank.nus.edu.sg/handle/10635/101507
ISSN: 17443091
DOI: 10.1107/S1744309111031812
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