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Two‐dimensional crystallization of membrane proteins: the lipid layer strategy
Author(s) -
Levy Daniel,
Chami Mohamed,
Rigaud Jean-Louis
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)02748-x
Subject(s) - crystallization , membrane protein , context (archaeology) , membrane , protein crystallization , lipid bilayer , electron crystallography , chemistry , materials science , nanotechnology , biophysics , biochemistry , biology , organic chemistry , physics , electron diffraction , diffraction , optics , paleontology
Due to the difficulty to crystallize membrane proteins, there is a considerable interest to intensify research topics aimed at developing new methods of crystallization. In this context, the lipid layer crystallization at the air/water interface, used so far for soluble proteins, has been recently adapted successfully to produce two‐dimensional (2D) crystals of membrane proteins, amenable to structural analysis by electron crystallography. Besides to represent a new alternative strategy, this approach gains the advantage to decrease significantly the amount of material needed in incubation trials, thus opening the field of crystallization to those membrane proteins difficult to surexpress and/or purify. The systematic studies that have been performed on different classes of membrane proteins are reviewed and the physico‐chemical processes that lead to the production of 2D crystals are addressed. The different drawbacks, advantages and perspectives of this new strategy for providing structural information on membrane proteins are discussed.