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Free keywords:
*Bacterial Outer Membrane Proteins/ch [Chemistry]; Bacterial Outer Membrane Proteins/ip [Isolation & Purification]; Crystallization; Image Processing, Computer-Assisted; Macromolecular Systems; *Membrane Proteins/ch [Chemistry]; Microscopy, Electron; Models, Molecular; Porins; Protein Conformation; Pseudomonas/ul [Ultrastructure]; Staining and Labeling; Support, Non-U.S. Gov't
Abstract:
The three-dimensional structure of the regular surface protein (p4 symmetry, lattice constant a = b = 10.5 nm) of Comamonas acidovorans has been determined to a resolution of about 1.5 nm by means of electron microscopy and image processing. Three-dimensional reconstructions were performed using native outer membranes and artificial two-dimensional crystals of the surface protein, which was selectively solubilized by deoxycholate and recrystallized on carbon films. The two-fold symmetric morphological complex is composed of two identical monomers which are in tight contact with the outer membrane and presumably anchored to it by a small hydrophobic domain.
