Crystallization and preliminary X-ray studies of TON_0559, a putative member of the haloacid dehalogenase (HAD) superfamily from Thermococcus onnurineus NA1

Protein Pept Lett. 2008;15(2):235-7. doi: 10.2174/092986608783489625.

Abstract

To elucidate the molecular basis underlying their broad substrate specificity and reaction mechanism of the enzymes belonging to the haloacid dehalogenase (HAD) superfamily, TON_0559, a putative HAD subfamily protein from a hyperthermophilic archaeon Thermococcus onnurineus NA1, was expressed, purified and crystallized. X-ray diffraction data were collected to 2.0 A resolution. The space group is C2, with unit cell parameters a = 121.2 A, b = 62.9 A, c = 37.5 A and beta= 106.5 degrees .

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Crystallization
  • Molecular Sequence Data
  • Substrate Specificity
  • Thermococcus / enzymology*
  • X-Ray Diffraction

Substances

  • Archaeal Proteins