Cloning, purification, crystallization and preliminary crystallographic analysis of acylphosphatase from Pyrococcus horikoshii OT3
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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Document Type: Research Article
Publication date: 2004-06-01