Cocrystallization and preliminary crystallographic analysis of an inactive MaoC-like hydratase mutant with the substrate crotonyl-CoA

无活性的MaoC样水合酶突变体与底物巴豆酰辅酶A的共结晶及初步晶体学分析

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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.

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