朝向肌动蛋白丝内肌动蛋白分子的排列。

Towards an alignment of the actin molecule within the actin filament.

作者信息

Smith P R, Fowler W E, Aebi U

出版信息

Ultramicroscopy. 1984;13(1-2):113-23. doi: 10.1016/0304-3991(84)90062-7.

Abstract

Electron micrographs of negatively stained actin filament paracrystals and single-layered filament rafts showing different interfilament spacings have been studied and three-dimensional reconstructions have been computed from them. Lateral ordering of the filaments in rafts was lost when interfilament spacings exceeded 8.5 nm, suggesting this distance as an upper limit for the filament diameter. Further, all reconstructions showed the same structural features at the 3 nm resolution level, except that the filaments from ordered single-layered rafts appeared 10-20% wider than those from multi-layered paracrystals. A comparison between electron microscopical and X-ray filament data, and synthetic filaments generated using different tentative molecular models and/or orientations for actin did not allow a single best model to be selected.

摘要

对负染肌动蛋白丝副晶体和显示不同丝间间距的单层丝筏的电子显微照片进行了研究，并据此计算出三维重建图像。当丝间间距超过8.5纳米时，筏中丝的横向有序性丧失，这表明该距离是丝直径的上限。此外，所有重建图像在3纳米分辨率水平上都显示出相同的结构特征，只是来自有序单层筏的丝比来自多层副晶体的丝宽10%-20%。电子显微镜数据与X射线丝数据之间的比较，以及使用不同的肌动蛋白暂定分子模型和/或取向生成的合成丝，都无法选出单一的最佳模型。