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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Purification, crystallization and preliminary X-ray crystallographic analysis of squid heavy meromyosin
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Purification, crystallization and preliminary X-ray crystallographic analysis of squid heavy meromyosin

机译：鱿鱼重肌球蛋白的纯化，结晶和初步X射线晶体学分析

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摘要

All muscle-based movement is dependent upon carefully choreographed interactions between the two major muscle components, myosin and actin. Regulation of vertebrate smooth and molluscan muscle contraction is myosin based (both are in the myosin II class), and requires the double-headed form of myosin. Removal of Ca2+ from these muscles promotes a relatively compact conformation of the myosin dimer, which inhibits its interaction with actin. Although atomic structures of single myosin heads are available, the structure of any double-headed portion of myosin, including the approximate to 375kDa heavy meromyosin (HMM), has only been visualized at low (approximate to 20 angstrom) resolution by electron microscopy. Here, the growth of three-dimensional crystals of HMM with near-atomic resolution (up to approximate to 5 angstrom) and their X-ray diffraction are reported for the first time. These crystals were grown in off-state conditions, that is in the absence of Ca2+ and the presence of nucleotide analogs, using HMM from the funnel retractor muscle of squid. In addition to the crystallization conditions, the techniques used to isolate and purify this HMM are also described. Efforts at phasing and improving the resolution of the data in order to determine the structure are ongoing.
机译：所有基于肌肉的运动都取决于精心设计的两种主要肌肉成分（肌球蛋白和肌动蛋白）之间的相互作用。脊椎动物平滑肌和软体动物肌肉收缩的调节是基于肌球蛋白的（均属于肌球蛋白II类），并且需要双头形式的肌球蛋白。从这些肌肉中去除Ca2 +可促进肌球蛋白二聚体的相对紧凑构象，从而抑制其与肌动蛋白的相互作用。尽管可获得单肌球蛋白头的原子结构，但只有通过电子显微镜才能观察到肌球蛋白的任何双头部分的结构，包括大约375kDa的重肌球蛋白（HMM），其分辨率都较低。在这里，首次报道了具有接近原子分辨率（高达约5埃）的HMM三维晶体的生长及其X射线衍射。这些晶体是使用鱿鱼的漏斗牵开器肌肉中的HMM在非状态条件下生长的，即在不存在Ca2 +和核苷酸类似物的情况下。除了结晶条件外，还描述了用于分离和纯化该HMM的技术。为了确定结构，正在逐步调整和改善数据的分辨率。

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