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• W2030488105 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." @default.
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• W2030488105 date "1985-05-01" @default.
• W2030488105 modified "2023-09-25" @default.
• W2030488105 title "Projected structure of the pore-forming OmpC protein from Escherichia coli outer membrane" @default.
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• W2030488105 doi "https://doi.org/10.1016/s0006-3495(85)83959-x" @default.
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