Open AccessCloning, purification, crystallization and preliminary X‐ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head‐to‐head hydrocarbon biosynthesis
Author(s) -
Frias Janice A.,
Goblirsch Brandon R.,
Wackett Lawrence P.,
Wilmot Carrie M.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110031751
Subject(s) - crystallization , biosynthesis , stenotrophomonas maltophilia , hydrocarbon , synchrotron , crystallography , x ray crystallography , chemistry , x ray , cloning (programming) , diffraction , stereochemistry , biochemistry , enzyme , biology , physics , organic chemistry , bacteria , optics , genetics , programming language , computer science , pseudomonas aeruginosa
OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X‐ray diffraction data have been collected to 3.4 Å resolution. The crystals belonged to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 98.8, c = 141.0 Å.