Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis
- PMID: 16511137
- PMCID: PMC1952463
- DOI: 10.1107/S1744309105019093
Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis
Abstract
The S-adenosylmethionine-dependent methyltransferase BchU is an enzyme involved in the bacteriochlorophyll c biosynthetic pathway and catalyzes methylation at the C-20 position of the chlorin moiety. Recombinant Chlorobium tepidum BchU overproduced in Escherichia coli was purified and crystallized by the hanging-drop vapour-diffusion method using ammonium sulfate as a precipitant. The crystals belonged to the hexagonal space group P6(1)22 or P6(5)22, with unit-cell parameters a = b = 81.5, c = 250.7 A. A native data set was collected to 2.27 A resolution using synchrotron radiation at SPring-8.
Figures



References
-
- Blankenship, R. E. & Matsuura, K. (2003). Light-Harvesting Antennas in Photosynthesis, edited by B. R. Green & W. W. Parson, pp. 195–217. Dordrecht: Kluwer Academic Publishers.
-
- Blankenship, R. E., Olson, J. M. & Miller, M. (1995). Anoxygenic Photosynthetic Bacteria, edited by R. E. Blankenship, M. T. Madigan & C. E. Bauer, pp. 399–435. Dordrecht: Kluwer Academic Publishers.
-
- Eisen, J. A. et al. (2002). Proc. Natl Acad. Sci. USA, 99, 9509–9514. - PubMed
-
- Frigaard, N. U. & Bryant, D. A. (2004). Arch. Microbiol.182, 265–276. - PubMed
-
- Frigaard, N. U., Chew, A. G. M., Li, H., Maresca, J. A. & Bryant, D. A. (2003). Photosynth. Res.78, 93–117. - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials