Stahlberg, HFotiadis, DScheuring, SRemigy, HBraun, TMitsuoka, KFujiyoshi, YEngel, A2020-02-132020-02-132020-02-132001-08-2810.1016/S0014-5793(01)02746-6https://infoscience.epfl.ch/handle/20.500.14299/165391Electron crystallography and atomic force microscopy allow the study of two-dimensional membrane protein crystals. While electron crystallography provides atomic scale three-dimensional density maps, atomic force microscopy gives insight into the surface structure and dynamics at sub-nanometer resolution. Importantly, the membrane protein studied is in its native environment and its function can be assessed directly. The approach allows both the atomic structure of the membrane protein and the dynamics of its surface to be analyzed. In this way, the function-related conformational changes can be assessed, thus providing a detailed insight on the molecular mechanisms of essential biological processes. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.text::journal::journal article::research article