Kensler R W, Levine R J
J Muscle Res Cell Motil. 1982 Sep;3(3):349-61. doi: 10.1007/BF00713042.
Thick filaments, isolated in their long conformation from unstimulated Limulus telson muscles, were shadowed with platinum or platinum-carbon and examined using electron microscopy and optical diffraction techniques. All filaments showed evidence of a right-handed surface helix, which had a major repeat at approx. 43 nm. In fortuitously oriented specimens the subunits, presumably crossbridges, which comprised the helical strands were clearly delineated. Optical transforms obtained from images of shadowed filaments confirmed the helical repeat at approx. 43 nm and could be readily interpreted as patterns expected from a one-surface view of the four-stranded filament structure we have previously reported. The striking resemblance between optically filtered images of shadowed filaments and the computed reconstruction of the one-surface filament further confirm our model for the myosin lattice of the Limulus thick filament.
从未受刺激的鲎尾节肌中分离出处于长构象的粗肌丝，用铂或铂 - 碳进行投影，并用电子显微镜和光学衍射技术进行检查。所有肌丝均显示出右手表面螺旋的迹象，其主要重复周期约为43纳米。在偶然取向的标本中，构成螺旋链的亚基（可能是横桥）清晰可辨。从投影肌丝图像获得的光学变换证实了约43纳米的螺旋重复，并且很容易被解释为我们先前报道的四链肌丝结构单表面视图所预期的图案。投影肌丝的光学滤波图像与单表面肌丝的计算重建之间的惊人相似性进一步证实了我们关于鲎粗肌丝肌球蛋白晶格的模型。
