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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Two-dimensional crystallization of intact F-ATP synthase isolated from bovine heart mitochondria
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Two-dimensional crystallization of intact F-ATP synthase isolated from bovine heart mitochondria

机译:从牛心脏线粒体分离的完整F-ATP合酶的二维结晶

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摘要

Mitochondrial F-ATP synthase produces the majority of ATP for cellular functions requiring free energy. The structural basis for proton motive force-driven rotational catalysis of ATP formation in the holoenzyme remains to be determined. Here, the purification and two-dimensional crystallization of bovine heart mitochondrial F-ATP synthase are reported. Two-dimensional crystals of up to 1 mm in size were grown by dialysis-mediated detergent removal from a mixture of decylmaltoside-solubilized 1,2-dimyristoyl-sn-glycero-3-phosphocholine and F-ATP synthase against a detergent-free buffer. A projection map calculated from an electron micrograph of a negatively stained two-dimensional crystal revealed unit-cell parameters of a = 185.0, b = 170.3 angstrom, gamma = 92.5 degrees.
机译:线粒体F-ATP合酶可产生大部分ATP,以实现需要自由能的细胞功能。质子动力驱动全酶中ATP形成的旋转催化的结构基础尚待确定。在此,报道了牛心脏线粒体F-ATP合酶的纯化和二维结晶。通过透析介导的去污剂从无麦芽糖苷溶解的1,2-二肉豆蔻酰基-sn-甘油-3-磷酸胆碱和F-ATP合酶的混合物中通过去污去污剂来生长最大尺寸为1 mm的二维晶体。从负染色二维晶体的电子显微照片计算得出的投影图揭示了a = 185.0,b = 170.3埃,γ= 92.5度的晶胞参数。

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