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|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|
|Source:||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|
|Appears in Collections:||Staff Publications|
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