Molecular cloning, expression, purification and crystallographic analysis of zebrafish THEM2
Copyright policy )Molecular cloning, expression, purification and crystallographic analysis of zebrafish THEM2
Thioesterase superfamily member 2 (THEM2) is essential for cell proliferation of mammalian cells. It belongs to the hotdog-fold thioesterase superfamily and catalyzes the hydrolysis of the thioester bonds of acyl-CoA in vitro. In this study, THEM2 protein from zebrafish (fTHEM2) was expressed in Escherichia coli and purified by Ni-affinity and gel-filtration chromatography. fTHEM2 crystals were obtained using the sitting-drop vapour-diffusion method with PEG 10 000 as precipitant. X-ray diffraction data were collected to 1.80 Å resolution using a synchrotron-radiation source. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a=77.1, b=74.4, c=96.6 Å, β=93.7°.
- Chinese Academy of Sciences China (People's Republic of)
- Institute of Biophysics China (People's Republic of)
Palmitoyl-CoA Hydrolase, X-Ray Diffraction, Escherichia coli, Animals, Acyl Coenzyme A, Cloning, Molecular, Zebrafish Proteins, Crystallization, Crystallography, X-Ray, Zebrafish
Palmitoyl-CoA Hydrolase, X-Ray Diffraction, Escherichia coli, Animals, Acyl Coenzyme A, Cloning, Molecular, Zebrafish Proteins, Crystallization, Crystallography, X-Ray, Zebrafish
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