Open AccessCrystallization and preliminary X‐ray diffraction study of BchU, a methyltransferase from Chlorobium tepidum involved in bacteriochlorophyll c biosynthesis
Author(s) -
Harada Jiro,
Wada Kei,
Yamaguchi Hitomi,
Ohoka Hirozo,
Tamiaki Hitoshi,
Fukuyama Keiichi
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105019093
Subject(s) - bacteriochlorophyll , biosynthesis , methylation , methyltransferase , ammonium sulfate , escherichia coli , crystallization , stereochemistry , chemistry , biochemistry , crystallography , biology , enzyme , organic chemistry , gene , photosynthesis
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 P 6 1 22 or P 6 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.