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Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3

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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 Å on a synchrotron-radiation source. The crystals belong to space group P3221, with approximate unit-cell parameters a = b = 86.6, c = 75.4 Å and two monomers in the asymmetric unit.
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Keywords: acylphosphatase

Document Type: Research Article

Publication date: 2004-06-01

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