Aebi U, Fowler W E, Isenberg G, Pollard T D, Smith P R
J Cell Biol. 1981 Nov;91(2 Pt 1):340-51. doi: 10.1083/jcb.91.2.340.
Crystalline sheets of Acanthamoeba actin induced by the trivalent lanthanide gadolinium exist in three different polymorphic forms, which show different striation patterns and surface topographies. We have called these different forms "rectangular" and "square" sheets, and "cylinders" and have shown that each of the three forms is constructed from common "basic" lattices associated in different ways. We have used image processing of electron micrographs to obtain a model for the actin molecule in projection to a resolution of 1.5 nm. The overall dimensions observed in these images are 5.6 x 3.3 x 4.5 nm, and the molecule itself appears distinctly bilobed with the two lobes separated by a cleft. actin monomers in the sheets are arranged with P2 symmetry and are therefore packed in a manner different from that of the molecules in actin filaments. Because approximately 35% of the surface area of the actin molecule is exposed on the surface of these sheets, the sheets should be useful to study the stoichiometric binding of actin-binding proteins to the actin molecule.
由三价镧系元素钆诱导形成的棘阿米巴肌动蛋白晶体片存在三种不同的多晶型形式,它们具有不同的条纹图案和表面形貌。我们将这些不同的形式称为“矩形”片和“方形”片以及“圆柱体”,并表明这三种形式中的每一种都是由以不同方式关联的常见“基本”晶格构成的。我们利用电子显微镜图像的图像处理技术获得了肌动蛋白分子投影模型,分辨率达到1.5纳米。在这些图像中观察到的整体尺寸为5.6×3.3×4.5纳米,分子本身明显呈双叶状,两叶由一个裂隙隔开。片中的肌动蛋白单体以P2对称性排列,因此其堆积方式与肌动蛋白丝中的分子不同。由于肌动蛋白分子约35%的表面积暴露在这些片的表面,这些片对于研究肌动蛋白结合蛋白与肌动蛋白分子的化学计量结合应该是有用的。