Abstract
Recently, a number of two-dimensional crystalline protein arrays have been described, Some of these occur in bacterial surface layers, others are derived from integral membrane proteins. The study of regularly arranged membrane proteins is obviously of great potential value for a better understanding of their structure, and thus of the relation of their structure with their function. The success of this approach has been illustrated recently with bacteriorhodopsin [6]. In the present report, an attempt is made to combine ultrastructural information with the results of biochemical and functional studies of a pore-forming protein from the outer membrane of E. coli. Its aim is to gain insight into its structural Organization and the State of its association in the membrane, despite the limited ultrastructural resolution available thus far [21].
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© 1980 Springer-Verlag Berlin Heidelberg
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Rosenbusch, J.P., Alkan, M., Regenass, M., Steven, A.C. (1980). Matrix Porin: a Periodically Arranged Pore Protein in the Outer Membrane of Escherichia coli . In: Baumeister, W., Vogell, W. (eds) Electron Microscopy at Molecular Dimensions. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-67688-8_1
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DOI: https://doi.org/10.1007/978-3-642-67688-8_1
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