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首页> 美国卫生研究院文献>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 ∼375 kDa heavy meromyosin (HMM), has only been visualized at low (∼20 Å) resolution by electron microscopy. Here, the growth of three-dimensional crystals of HMM with near-atomic resolution (up to ∼5 Å) 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（两者均属于肌球蛋白II类），并且需要双头形式的肌球蛋白。从这些肌肉中去除Ca 2 + 会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，但肌球蛋白的任何双头部分的结构，包括〜375 kDa重肌球蛋白（HMM），都只能通过电子显微镜以低分辨率（〜20Å）观察到。在这里，首次报道了具有接近原子分辨率（至多5Å）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，即不存在Ca 2 + 和核苷酸类似物。除结晶条件外，还描述了用于分离和纯化该HMM的技术。为了确定结构，正在进行逐步调整和提高数据分辨率的工作。

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