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  The three-dimensional structure of the regular surface protein of Comamonas acidovorans derived from native outer membranes and reconstituted two-dimensional crystals

Engelhardt, H., Gerbl-Rieger, S., Santarius, U., & Baumeister, W. (1991). The three-dimensional structure of the regular surface protein of Comamonas acidovorans derived from native outer membranes and reconstituted two-dimensional crystals. Molecular Microbiology., 5(7), 1695-1702.

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Engelhardt, H.1, Author              
Gerbl-Rieger, S., Author
Santarius, U.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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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.

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 Dates: 1991
 Publication Status: Published in print
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 Identifiers: eDoc: 318632
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Title: Molecular Microbiology.
Source Genre: Journal
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Pages: - Volume / Issue: 5 (7) Sequence Number: - Start / End Page: 1695 - 1702 Identifier: -