PMID:15159579

Citation	Miyazono, KI, Kudo, N and Tanokura, M (2004) Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3. Acta Crystallogr. D Biol. Crystallogr. 60:1135-6
Abstract	Acylphosphatase is one of the smallest enzymes and catalyzes the hydrolysis of the carboxy-phosphate bond. An extremely thermostable acylphosphatase from a hyperthermophilic archaea, Pyrococcus horikoshii OT3, has been cloned, expressed in Escherichia coli, purified and crystallized using the sitting-drop vapour-diffusion method with potassium/sodium tartrate as the precipitant at pH 5.5. X-ray diffraction data have been collected to a highest resolution of 1.72 angstroms on a synchrotron-radiation source. The crystals belong to space group P3(2)21, with approximate unit-cell parameters a = b = 86.6, c = 75.4 angstroms and two monomers in the asymmetric unit.
Links	PubMed Online version:10.1107/S0907444904007735
Keywords	Acid Anhydride Hydrolases/chemistry; Acid Anhydride Hydrolases/genetics; Acid Anhydride Hydrolases/isolation & purification; Carbon/chemistry; Cloning, Molecular; Crystallization; Crystallography, X-Ray/methods; Diffusion; Escherichia coli/metabolism; Hydrogen-Ion Concentration; Models, Statistical; Phosphates/chemistry; Pyrococcus horikoshii/enzymology; Synchrotrons; Tartrates/pharmacology; X-Ray Diffraction
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