Two‐dimensional crystallization of membrane proteins: the lipid layer strategy

FEBS Letters

Rigaud, Jean-Louis¹  Levy, Daniel¹  Chami, Mohamed¹ 

[1] Institut Curie, Section de Recherche, UMR-CNRS 168 and LRC-CEA 8, 11 Rue Pierre et Marie Curie, 75231 Paris Cedex 05, France

关键词: Two-dimensional crystallization;    Membrane protein;    Lipid layer;    Lipid ligand;    Ni2+-NTA;    nickel-chelated nitriloacetic acid;    2D;    two-dimensional;    3D;    three-dimensional;    cmc;    critical micellar concentration;    His;    histidine;    RLM;    reflected light microscopy;   

DOI  :  10.1016/S0014-5793(01)02748-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown