Toyoshima C, Wakabayashi T
J Biochem. 1979 Dec;86(6):1887-90. doi: 10.1093/oxfordjournals.jbchem.a132712.
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.
通过对负染标本的电子显微照片进行重构,得到了肌动蛋白与胰凝乳蛋白酶消化的肌球蛋白亚片段-1“僵直”复合物的三维图像。数据在径向延伸至20埃,轴向延伸至26埃。重构图像使我们能够推断出肌球蛋白亚片段-1主要部分的长轴与肌动蛋白螺旋轴之间的夹角。亚片段-1分子以一种构型附着在肌动蛋白丝上,在这种构型中,它们相对于垂直于肌动蛋白螺旋轴的平面仅倾斜约15度。文中讨论了该倾斜角小于普遍接受值的意义。