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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Purification, crystallization and preliminary crystallographic analysis of the globular domain of the human type V myosin Myo5a
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Purification, crystallization and preliminary crystallographic analysis of the globular domain of the human type V myosin Myo5a

机译：人V型肌球蛋白Myo5a球状结构域的纯化，结晶和初步晶体学分析

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摘要

Type V myosins constitute the main cargo-transporting class of myosin motors in higher eukaryotes. They are mainly defined by their C-terminal globular domain, which is required for cargo binding as well as for motor auto-inhibition in the absence of cargo. To date, high-resolution structures only exist for globular domains from yeast. Since the majority of cellular cargoes in yeast are very different from the cargoes in higher eukaryotes, structural insights into the domain organization of globular domains from human type V myosins are important. The globular domain of human Myo5a was cloned, expressed and crystallized and data sets were collected. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 75.04, b = 86.70, c = 131.41 angstrom, alpha = beta = gamma = 90 degrees, and diffracted with data-collection quality to 2.5 angstrom resolution.
机译：V型肌球蛋白是高级真核生物中肌球蛋白马达的主要运输类别。它们主要由它们的C末端球状结构域定义，这对于货物绑定以及不存在货物时的运动自动抑制是必需的。迄今为止，高分辨率结构仅存在于来自酵母的球状结构域中。由于酵母中的大多数细胞货物与高级真核生物中的货物非常不同，因此对人V型肌球蛋白的球状结构域的域组织的结构洞察非常重要。克隆，表达和结晶人Myo5a的球状结构域，并收集数据集。晶体属于空间群P2（1）2（1）2（1），其晶胞参数a = 75.04，b = 86.70，c = 131.41埃，alpha = beta =伽马= 90度，并衍射了数据-采集质量达到2.5埃分辨率。

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