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Detergent‐free membrane protein crystallization
Author(s) -
Nollert Peter,
Royant Antoine,
Pebay-Peyroula Eva,
Landau Ehud M.
Publication year - 1999
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(99)01014-5
Subject(s) - bacteriorhodopsin , mosaicity , crystallization , protein crystallization , crystallography , membrane protein , chemistry , phase (matter) , halobacterium salinarum , membrane , resolution (logic) , diffraction , x ray crystallography , biochemistry , physics , optics , organic chemistry , artificial intelligence , computer science
A comprehensive understanding of structure‐function relationships of proteins requires their structures to be elucidated to high resolution. With most membrane proteins this has not been accomplished so far, mainly because of their notoriously poor crystallizability. Here we present a completely detergent‐free procedure for the incorporation of a native purple membrane into a monoolein‐based lipidic cubic phase, and subsequent crystallization of three‐dimensional bacteriorhodopsin crystals therein. These crystals exhibit comparable X‐ray diffraction quality and mosaicity, and identical crystal habit and space group to those of bacteriorhodopsin crystals that are grown from detergent‐solubilized protein in cubic phase.