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The three-dimensional structure of the regular surface protein of Comamonas acidovorans derived from native outer
H Engelhardt1, S Gerbl-Rieger, U Santarius
1Max-Plank-Institute für Biochemie, Martinsried, Germany.
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.