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


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 A resolution data set was collected using synchrotron radiation. The TON-HolPase crystals belonged to space group P222(1), with unit-cell parameters a = 40.88, b = 46.89, c = 148.03 A. Assuming the presence of one molecule in the asymmetric unit, the solvent content was estimated to be about 48.3%.

SUBMITTER: Jung HI 

PROVIDER: S-EPMC2675587 | biostudies-literature | 2009 May

REPOSITORIES: biostudies-literature

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

Jung Ha Il HI   Lee Hyun Sook HS   An Young Jun YJ   Cho Yona Y   Lee Jung Hyun JH   Kang Sung Gyun SG   Cha Sun Shin SS  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090424 Pt 5


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 A resolution data set was  ...[more]

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