Ueki T, Mitsui T, Nikaido H
J Biochem. 1979 Jan;85(1):173-82. doi: 10.1093/oxfordjournals.jbchem.a132307.
X-ray diffraction studies were carried out on the outer membranes of various strains of Salmonella typhimurium. Ten distinct diffraction peaks which seem to be caused by protein assemblies were observed for most strains. Three small-angle reflections were used to determine an average structure of the protein assembly in the outer membrane of mutant HN202. An electron density distribution of the averaged assembly was obtained by means of the Fourier-Bessel transform. It has a diameter of about 100A, in agreement with the results of electron microscope observations (Smit, Kamio, and Nikaido (1975) J. Bacteriol. 124, 942--958), and exhibits a low electron density region at its center, suggesting the presence of a pore, as predicted on the basis of transmembrane transport experiments (Nakae (1976) J. Biol. Chem. 251, 2176--2178).
对多种鼠伤寒沙门氏菌菌株的外膜进行了X射线衍射研究。大多数菌株观察到十个明显的衍射峰，这些峰似乎由蛋白质组装体引起。利用三个小角反射来确定突变体HN202外膜中蛋白质组装体的平均结构。通过傅里叶-贝塞尔变换获得了平均组装体的电子密度分布。其直径约为100埃，与电子显微镜观察结果一致（斯密特、神尾和二木户（1975年）《细菌学杂志》124卷，942 - 958页），并且在其中心呈现出低电子密度区域，这表明存在一个孔，正如基于跨膜运输实验所预测的那样（中江（1976年）《生物化学杂志》251卷，2176 - 2178页）。
