title: Cloning, purification, crystallization and preliminary X-ray diffraction of the OleC protein from Stenotrophomonas maltophilia involved in head-to-head hydrocarbon biosynthesis.
abstract: OleC, a biosynthetic enzyme involved in microbial hydrocarbon biosynthesis, has been crystallized. Synchrotron X-ray diffraction data have been collected to 3.4 A resolution. The crystals belonged to space group P3(1)21 or P3(2)21, with unit-cell parameters a=b=98.8, c=141.0 A.
authors.affiliation: University of Minnesota, Minneapolis, MN, USA.
authors.forename: Janice A
authors.initials: JA
authors.lastname: Frias
authors.forename: Brandon R
authors.initials: BR
authors.lastname: Goblirsch
authors.forename: Lawrence P
authors.initials: LP
authors.lastname: Wackett
authors.forename: Carrie M
authors.initials: CM
authors.lastname: Wilmot
mesh_terms: D000217:Acyltransferases / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D020615:Stenotrophomonas maltophilia / Q000201:enzymology*
chemical_list: D000217:Acyltransferases; C034919:acyl protein synthetase
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