title: Cocrystallization and preliminary crystallographic analysis of an inactive MaoC-like hydratase mutant with the substrate crotonyl-CoA.
abstract: MaoC-like hydratase (MaoC) is a recently identified enzyme involved in the biosynthetic pathway of polyhydroxyalkanoates (PHAs), which are completely biodegradable polymers used to produce green plastics. The inactive mutant D194N-MaoC was crystallized in the presence of the substrate crotonyl-CoA. Crystals were grown in a number of conditions, but only those produced using 20%(v/v) ethylene glycol were suitable for structural studies. Data were collected to 2.10 Å resolution using X-radiation and the crystal belonged to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 81.40, b = 82.58, c = 123.99 Å.
authors.affiliation: Department of Plant Pathology, Shandong Agricultural University, Tai'an 271018, People's Republic of China.
authors.forename: Huizheng
authors.initials: H
authors.lastname: Wang
authors.forename: Jie
authors.initials: J
authors.lastname: Zhu
authors.forename: Weiwei
authors.initials: W
authors.lastname: Song
authors.forename: Xiuguo
authors.initials: X
authors.lastname: Zhang
mesh_terms: D000214:Acyl Coenzyme A / Q000737:chemistry* / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D004746:Enoyl-CoA Hydratase / Q000737:chemistry* / Q000378:metabolism; D004789:Enzyme Activation; D009154:Mutation; D010838:Phytophthora / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D000214:Acyl Coenzyme A; C010701:crotonyl-coenzyme A; D004746:Enoyl-CoA Hydratase