ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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%.
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