ARCHIVES
VOL. 1, ISSUE 4 (2014)
Crystallization and preliminary X-ray diffraction analysis of SibL, a SAM-dependent C-methyltransferase from Streptosporangium sibiricum
Authors
Pin-Kuei Fu, Shih-Ting Tseng, Sheng-Chia Chen, Jai-Shin Liu, Ya-Ping Huang, Chia-Shin Yang, Cheng-Yang Huang and Yeh Chen
Abstract
SibL is an S-adenosyl-L-methionine (SAM)-dependent C-methyltransferase (CMT) involved in sibiromycin biosynthesis. Specifically, it establishes the C8 methylation step in the biosynthesis pathway, and the resultant methyl group is important for maturation of the antitumor antibiotic. Here, we purified and crystallized SibL from Streptosporangium sibiricum using the sitting-drop vapor-diffusion method. The crystals diffracted to a resolution of 2.9 Ã… and belonged to orthorhombic space group F222, with unit-cell parameters a = 102.93, b = 295.42, c = 322.23 Ã…. Determining the structure will provide insights into how SibL methylates 3-hydroxykynurenine (3HK).
Download
Pages:19-23
How to cite this article:
Pin-Kuei Fu, Shih-Ting Tseng, Sheng-Chia Chen, Jai-Shin Liu, Ya-Ping Huang, Chia-Shin Yang, Cheng-Yang Huang and Yeh Chen "Crystallization and preliminary X-ray diffraction analysis of SibL, a SAM-dependent C-methyltransferase from Streptosporangium sibiricum". International Journal of Multidisciplinary Research and Development, Vol 1, Issue 4, 2014, Pages 19-23
Download Author Certificate
Please enter the email address corresponding to this article submission to download your certificate.
