Hebert H, Skriver E, Söderholm M, Maunsbach A B
Department of Cell Biology, University of Aarhus, Denmark.
J Ultrastruct Mol Struct Res. 1988 Jul;100(1):86-93. doi: 10.1016/0889-1605(88)90061-4.
Electron microscopy and image processing were used to reconstruct a three-dimensional model of membrane-bound monomeric renal Na,K-ATPase from negatively stained two-dimensional crystals of the p1 type. Correlation methods were applied to obtain projection averages which were aligned by a phase difference minimization procedure. The self-consistency of the reconstruction process was high as determined by correlation between experimental projections and projections of the calculated model. The three-dimensional model of the Na,K-ATPase promoter in the p1 crystal form contains three characteristic domains, a protein dense ellipsoid, a small globular stain deficient domain, and a connecting low-contrast region. The latter is thought to correspond to the lipid-penetrating part of the Na,K-ATPase promoter. The location of this domain gives the protein an asymmetric distribution in the bilayer so that it is exposed primarily on one side proposed to correspond to the intracellular face.
利用电子显微镜和图像处理技术，从p1型负染色二维晶体中重建了膜结合单体肾钠钾ATP酶的三维模型。应用相关方法获得投影平均值，并通过相位差最小化程序进行对齐。根据实验投影与计算模型投影之间的相关性确定，重建过程的自洽性很高。p1晶体形式的钠钾ATP酶启动子的三维模型包含三个特征结构域，一个蛋白质密集的椭球体、一个小的球状染色缺陷结构域和一个连接的低对比度区域。后者被认为对应于钠钾ATP酶启动子的脂质穿透部分。该结构域的位置使蛋白质在双层中呈不对称分布，因此它主要暴露在一侧，推测对应于细胞内面。
