X-ray diffraction studies of outer membranes of Salmonella typhimurium

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).