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Purification and crystallization of the entire recombinant subunit E of the energy producer A1Ao ATP synthase

机译:能量产生剂A1Ao ATP合酶的整个重组亚基E的纯化和结晶

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摘要

A1Ao ATP synthases are the major energy producers in archaea. Subunit E of the stator domain of the ATP synthase from Pyrococcus horikoshii OT3 was cloned, expressed and purified to homogeneity. The monodispersed protein was crystallized by vapour diffusion. A complete diffraction data set was collected to 3.3 Å resolution with 99.4% completeness using a synchrotron-radiation source. The crystals belonged to space group I4, with unit-cell parameters a = 112.51, b = 112.51, c = 96.25 Å, and contained three molecules in the asymmetric unit.
机译:A 1 A o ATP合酶是古生菌的主要能量产生者。克隆,表达和纯化了来自火球菌OT3的ATP合酶的定子结构域的亚基E。通过蒸汽扩散使单分散的蛋白质结晶。使用同步辐射源将完整的衍射数据集以99.4%的完整性收集到3.3Å分辨率。晶体属于I4空间群,晶胞参数a = 112.51,b = 112.51,c = 96.25,并且在不对称单元中包含三个分子。

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