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X‐Ray Structure of Bacteriorhodopsin at 2.5 Å Resolution
Author(s) -
Hucho Ferdinand
Publication year - 1998
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/(sici)1521-3773(19980619)37:11<1518::aid-anie1518>3.0.co;2-s
Subject(s) - bacteriorhodopsin , crystallization , resolution (logic) , crystallography , synchrotron , crystal structure , protein crystallization , electron crystallography , membrane protein , chemistry , physics , membrane , diffraction , optics , electron diffraction , computer science , biochemistry , organic chemistry , artificial intelligence
Microfocussed X‐rays produced by an electron synchrotron were essential for the first structure elucidation of protein crystals having extremely small dimensions (5×20–40 μm). A further prerequisite for the successful crystal structure analysis of bacteriorhodopsin was a novel crystallization method using a lipid matrix. These methodological breakthroughs pave the way for further advances in structure determinations of membrane proteins.