Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1

Ha Il Jung, Hyun Sook Lee, Young Jun An, Yona Cho, Jung Hyun Lee, Sung Gyun Kang, Sun Shin Cha

Research output: Contribution to journalArticlepeer-review

Abstract

The TON-0887 gene product from Thermococcus onnurineus NA1 is a 240-residue protein that has histidinol-phosphate phosphatase (HolPase) activity. According to analysis of its primary structure, the TON-0887 gene product is a monofunctional HolPase that belongs to the DDDD superfamily. This contrasts with the generally accepted classification that bifunctional HolPases belong to the DDDD superfamily. The TON-0887 gene product was purified and crystallized at 295 K. A 2.2 Å resolution data set was collected using synchrotron radiation. The TON-HolPase crystals belonged to space group P2221, with unit-cell parameters a = 40.88, b = 46.89, c = 148.03 Å. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 48.3%.

Original languageEnglish
Pages (from-to)472-474
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number5
DOIs
StatePublished - 2009

Keywords

  • Histidinol-phosphate phosphatase
  • Thermococcus onnurineus NA1

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