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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 |
Appears in Collections: | Staff Publications |
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