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An Approach To Prepare Membrane Proteins for Single‐Molecule Imaging
Author(s) -
Cisneros David A.,
Muller Daniel J.,
Daud Sofian M.,
Lakey Jeremy H.
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200504506
Subject(s) - atomic force microscopy , orientation (vector space) , membrane , membrane protein , nanotechnology , crystallography , molecule , microscopy , cysteine , quality (philosophy) , chemistry , computer science , biophysics , physics , materials science , biochemistry , optics , biology , mathematics , enzyme , organic chemistry , geometry , quantum mechanics
Observed from above : A cysteine mutation in a membrane protein enables it to be fixed in a defined orientation on flat gold surfaces (see picture, left). Subsequent coassembly with thiolipids produces clearly defined, immobilized proteins. Analysis by atomic force microscopy provides topographs of similar quality to those revealed from 2D crystals.