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- Publisher
- Wiley
- Copyright
- Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309105019093
- pmid
- 16511137
- Publisher site
- See Article on Publisher Site
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 P6122 or P6522, 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.
Journal
Acta Crystallographica Section F – Wiley
Published: Jul 1, 2005