Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. I. Tilt angle of myosin subfragment-1 in the rigor complex.
Three-dimensional image analysis of the complex of thin filaments and myosin molecules from skeletal muscle. I. Tilt angle of myosin subfragment-1 in the rigor complex.
复制标题
骨骼肌细丝和肌球蛋白分子复合物的三维图像分析。
DOI：
10.1093/oxfordjournals.jbchem.a132712
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发表时间：
1979
影响因子：
2.7
通讯作者：
T. Wakabayashi
中科院分区：
文献类型：
--
作者：
C. Toyoshima;T. Wakabayashi
从负染色标本的电子显微照片中重建了肌动蛋白和胰凝乳蛋白酶肌球蛋白亚片段-1的“僵硬”复合物的三维图像。数据输出为径向20 A和轴向26 A。重建的图像使我们能够推断出肌球蛋白亚片段-1的主要部分的主轴和肌动蛋白螺旋轴之间的角度。亚片段-1分子附着在肌动蛋白丝上，其构型与垂直于肌动蛋白螺旋轴的平面仅倾斜约15度。讨论了比通常接受的值更小的倾斜角的含义。
A three-dimensional image of the "rigor" complex of actin and chymotryptic myosin subfragment-1 was reconstituted from electron micrographs of negatively stained specimens. Data went out to 20 A radially and 26 A axially. The reconstituted images allowed us to deduce the angle between the major axis of the main part of myosin subfragment-1 and the axis of the actin helix. The subfragment-1 molecules were attached to the actin filament in a configuration in which they were tilted by only about 15 degrees from the plane perpendicular to the axis of the actin helix. The implication of the smaller tilt angle than the commonly accepted value is discussed.