Crystallization and preliminary X-ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis

Journal Article · Fri Jul 01 04:00:00 EDT 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309105019093· OSTI ID:22356148

Harada, Jiro ^[1]; Wada, Kei; Yamaguchi, Hitomi; Oh-oka, Hirozo ^[2]; Tamiaki, Hitoshi ^[1]; Fukuyama, Keiichi ^[2]

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1. Department of Bioscience and Biotechnology, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga 525-8577 (Japan)
2. 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, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 7 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
AMMONIUM SULFATES
CRYSTALLIZATION
CRYSTALS
DIFFUSION
ESCHERICHIA COLI
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
X-RAY DIFFRACTION