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Science 7 April 1995:
Vol. 268. no. 5207, pp. 92 - 94
DOI: 10.1126/science.7701347
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Articles

Science, Vol 268, Issue 5207, 92-94
Copyright © 1995 by American Association for the Advancement of Science

articles

Native Escherichia coli OmpF porin surfaces probed by atomic force microscopy

FA Schabert, C Henn, and A Engel

Maurice E. Muller Institute for Microscopic Structural Biology, Universitat Basel, Switzerland.

Topographs of two-dimensional porin OmpF crystals reconstituted in the presence of lipids were recorded in solution by atomic force microscopy (AFM) to a lateral resolution of 10 angstroms and a vertical resolution of 1 angstrom. Protein-protein interactions were demonstrated on the basis of the AFM results and earlier crystallographic findings. To assess protein-lipid interactions, the bilayer was modeled with kinked lipids by fitting the head groups to contours determined with AFM. Finally, two conformations of the extracellular porin surface were detected at forces of 0.1 nanonewton, demonstrating the potential of AFM to monitor conformational changes with high resolution.


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