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Two‐dimensional crystals: a powerful approach to assess structure, function and dynamics of membrane proteins
Author(s) -
Stahlberg Henning,
Fotiadis Dimitrios,
Scheuring Simon,
Rémigy Hervé,
Braun Thomas,
Mitsuoka Kaoru,
Fujiyoshi Yoshinori,
Engel Andreas
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02746-6
Subject(s) - electron crystallography , membrane protein , atomic force microscopy , atomic units , chemical physics , molecular dynamics , chemistry , membrane , resolution (logic) , electron microscope , function (biology) , nanometre , protein structure , crystallography , biophysics , nanotechnology , materials science , physics , electron diffraction , computational chemistry , diffraction , biology , computer science , biochemistry , optics , quantum mechanics , composite material , artificial intelligence , evolutionary biology
Electron 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.