Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis
- Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525-8577 (Japan)
- Department of Biology, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 (Japan)
Recombinant BchU from C. tepidum has been crystallized. Crystals diffract to 2.27 Å using synchrotron radiation at SPring-8 and belong to space group P6{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = b = 81.5, c = 250.7 Å. 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{sub 1}22 or P6{sub 5}22, with unit-cell parameters a = b = 81.5, c = 250.7 Å. A native data set was collected to 2.27 Å resolution using synchrotron radiation at SPring-8.
- OSTI ID:
- 22356148
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 7; Other Information: PMCID: PMC1952463; PMID: 16511137; PUBLISHER-ID: vr5042; OAI: oai:pubmedcentral.nih.gov:1952463; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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