Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans.

ABSTRACT: 3-Hydroxyacyl-CoA dehydrogenase (HAD; EC 1.1.1.35) is the enzyme that catalyzes the third step in fatty-acid β-oxidation, oxidizing the hydroxyl group of 3-hydroxyacyl-CoA to a keto group. The 3-hydroxyacyl-CoA dehydrogenase from Caenorhabditis elegans (cHAD) was cloned, overexpressed in Escherichia coli and purified to homogeneity for crystallography. Initial crystals were obtained by the hanging-drop vapour-diffusion method. Optimization of the precipitant concentration and the pH yielded two types of well diffracting crystals with parallelepiped and cuboid shapes, respectively. Complete diffraction data sets were collected and processed from both crystal types. Preliminary crystallographic analysis indicated that the parallelepiped-shaped crystal belonged to space group P1, while the cu

SUBMITTER: Xu Y 

PROVIDER: S-EPMC3660890 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature