Please use this identifier to cite or link to this item:
|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.
|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|
Show full item record
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.