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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318632.0, MPI für Biochemie / Structural Biology (W. Baumeister)
The three-dimensional structure of the regular surface protein of Comamonas acidovorans derived from native outer membranes and reconstituted two-dimensional crystals
Authors:Engelhardt, H.; Gerbl-Rieger, S.; Santarius, U.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1991
Title of Journal:Molecular Microbiology.
Volume:5
Issue / Number:7
Start Page:1695
End Page:1702
Audience:Not Specified
Abstract / Description: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.
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
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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