PUBLICATION

Molecular cloning, expression, purification and crystallographic analysis of zebrafish THEM2

Authors
Li, H., Gao, F., Yu, S., Jia, M., and Gong, W.
ID
ZDB-PUB-121206-12
Date
2012
Source
Acta crystallographica. Section F, Structural biology and crystallization communications   68(12): 1525-1528 (Journal)
Registered Authors
Keywords
THEM2, thioesterase superfamily member 2, Danio rerio
MeSH Terms
  • Acyl Coenzyme A/chemistry
  • Animals
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli/genetics
  • Escherichia coli/metabolism
  • Palmitoyl-CoA Hydrolase/chemistry*
  • Palmitoyl-CoA Hydrolase/genetics
  • Palmitoyl-CoA Hydrolase/isolation & purification
  • X-Ray Diffraction
  • Zebrafish/genetics
  • Zebrafish/metabolism*
  • Zebrafish Proteins/chemistry*
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/isolation & purification*
PubMed
23192039 Full text @ Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Abstract

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°.

Genes / Markers
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Human Disease / Model
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