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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii.
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Crystallization and preliminary crystallographic analysis of an acylphosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii.

机译：结晶和初步的晶体分析acylphosphatase的hyperthermophilic archaeon海床horikoshii。

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摘要

Acylphosphatases catalyse the hydrolysis of the carboxyl phosphate bond in metabolites such as acetyl phosphate, 1,3-bisphosphoglycerate, succinoyl phosphate and carbamoyl phosphate. In this study, acylphosphatase (91 residues) from the hyperthermophilic archaeon Pyrococcus horikoshii has been cloned, overexpressed, purified and crystallized using the sitting-drop vapour-diffusion method using sodium formate as a precipitant at 289 K. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 85.65, c = 75.51 A. The asymmetric unit contains two molecules of acylphosphatase, with a corresponding crystal volume per protein weight of 3.9 A Da(-1) and a solvent content of 68.6%. A data set diffracting to 1.6 A resolution was collected from a single crystal at 100 K.
机译：Acylphosphatases催化的水解羧基等代谢物的磷酸键3-bisphosphoglycerate乙酰磷酸,1日,succinoyl磷酸盐和[氨基甲酰磷酸。从这项研究中,acylphosphatase(91残留物)的hyperthermophilic archaeon海床horikoshii被克隆,过表达,使用sitting-drop提纯和结晶使用甲酸钠作为vapour-diffusion方法沉淀剂在289 K。空间群P3(2) 21日晶胞参数A = b = 85.65, c = 75.51。包含两个分子acylphosphatase,相应的蛋白质晶体体积/重量达3.9(1)和溶剂含量的68.6%。数据集衍射分辨率1.6收集的100 K的单晶。

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