Rayns D G
J Microsc. 1975 Mar;103(2):215-26. doi: 10.1111/j.1365-2818.1975.tb03897.x.
Myofilament structure was studied in freeze-etch replicas of unfixed, glycerinated beef cardiac muscle. The information which is revealed depends upon the direction of metal shadowing in relation to the filament axis. Shadows oblique to this axis reveal that the outer surface of a longitudinal half of a thick filament comprises three, sometimes four, rows of myosin molecules. These molecules are generally assembled in a braided manner with both left and right-handed helical components. Occasionally a more parallel to the myofilament axis reveal cross-bridges linking thick and thin filaments. These bridges are readily detectable by optical diffraction techniques, giving an axial bridge spacing of approximately 40 nm. In unetched preparations cross bridges appear as vertical rows of beads. In all replicas the effects of plastic deformation of proteins must be considered.
在未固定的甘油处理的牛肉心肌的冷冻蚀刻复制品中研究了肌丝结构。所揭示的信息取决于金属阴影相对于细丝轴的方向。与该轴倾斜的阴影表明，粗丝纵向一半的外表面由三排，有时四排肌球蛋白分子组成。这些分子通常以编织方式组装，同时包含左手和右手螺旋成分。偶尔，与肌丝轴更平行的方向会显示连接粗丝和细丝的横桥。这些桥很容易通过光学衍射技术检测到，轴向桥间距约为40nm。在未蚀刻的制剂中，横桥表现为垂直的珠子排。在所有复制品中，都必须考虑蛋白质塑性变形的影响。
