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首页> 外文期刊>Journal of Molecular Biology >PRELIMINARY CRYOCRYSTALLOGRAPHIC STUDY OF THE MITOCHONDRIAL CYTOCHROME BC(1) COMPLEX - IMPROVED CRYSTALLIZATION AND FLASH-COOLING OF A LARGE MEMBRANE PROTEIN
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PRELIMINARY CRYOCRYSTALLOGRAPHIC STUDY OF THE MITOCHONDRIAL CYTOCHROME BC(1) COMPLEX - IMPROVED CRYSTALLIZATION AND FLASH-COOLING OF A LARGE MEMBRANE PROTEIN

机译：线粒体细胞色素BC（1）的复杂的初步结晶学研究-改进的结晶和大膜蛋白的快速冷却

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Ubiquinol-cytochrome c reductase is a crucial integral membrane protein in the mitochondrial respiratory cycle. Eleven subunits containing three cytochrome heme groups and a 2Fe-2S Rieske center make up this 240 kDa enzyme complex. Previously, many different crystal forms of the bc(1) complex have displayed diffraction to as far as 4.5 Angstrom. However, rapid degradation of the protein in the X-ray beam at room temperature has obstructed the collection of a full data set from a single crystal. As slight heterogeneities between crystals severely hampered merging of data from different crystals, we sought a method to stabilize the protein crystal in the X-ray beam in order to collect a full data set from one crystal sample. To this end, water soluble protein crystals are frequently flash-cooled to cryogenic temperatures; however, there is no report of cryocrystallography for membrane proteins. In this communication, we report on a successful experiment in which flash-cooled bc(1) membrane protein crystals have given rise to sustained diffraction over a 60 hour data collection period at a synchrotron source. Furthermore, we present an improved purification and crystallization protocol yielding crystals readily diffracting out to 3.3 Angstrom. These results should greatly aid in the future realization of the molecular structure of the bc(1) complex as well as other membrane proteins. (C) 1995 Academic Press Limited [References: 30]
机译：泛醇-细胞色素c还原酶是线粒体呼吸循环中至关重要的完整膜蛋白。包含三个细胞色素血红素基团和2Fe-2S Rieske中心的11个亚基组成了这个240 kDa的酶复合物。以前，bc（1）络合物的许多不同晶体形式都显示出高达4.5埃的衍射。但是，室温下X射线束中蛋白质的快速降解阻碍了从单晶收集完整数据集。由于晶体之间的微小异质性严重阻碍了来自不同晶体的数据合并，因此我们寻求一种稳定X射线束中蛋白质晶体的方法，以便从一个晶体样品中收集完整的数据集。为此，经常将水溶性蛋白质晶体快速冷却至低温。但是，没有关于膜蛋白的冷冻结晶学的报道。在此交流中，我们报告了一个成功的实验，其中，在同步加速器源上，快速冷却的bc（1）膜蛋白晶体在60小时的数据收集期内引起了持续衍射。此外，我们提出了一种改进的纯化和结晶方案，使晶体容易衍射到3.3埃。这些结果将大大有助于bc（1）配合物以及其他膜蛋白的分子结构的未来实现。 （C）1995 Academic Press Limited [参考：30]

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