Projected Structure of the Pore-forming OmpC Protein from Escherichia Coli Outer Membrane

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 1985 May 1

PMID 3893556

Citations 3

Authors

C F Chang

S Mizushima

R M Glaeser

Affiliations

Soon will be listed here.

Abstract

A single-projection structure analysis of a bacterial outer membrane protein, OmpC, has been carried out by electron microscopy of frozen hydrated specimens. Two distinct crystal polymorphs have been observed in the frozen-hydrated samples, and projection structures of both forms have been obtained to a resolution of 13.5 A. Preliminary examination of negatively stained samples revealed the expected, trimeric appearance of pores in the OmpC specimens. Electron microscopy of unstained, frozen-hydrated OmpC reveals the trimeric pore structure with equal clarity. In addition, the overall molecular envelope of the protein is readily discerned, and a major lipid-containing domain can also be seen. Because of the small coherent patch size, mosaic disorder, and unpredictable polymorphism of the presently available specimens, three-dimensional reconstruction of frozen-hydrated OmpC has not been carried out.

Citing Articles

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