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Membrane protein crystallization from lipidic phases.

Authors :
Johansson LC
Wöhri AB
Katona G
Engström S
Neutze R
Source :
Current opinion in structural biology [Curr Opin Struct Biol] 2009 Aug; Vol. 19 (4), pp. 372-8. Date of Electronic Publication: 2009 Jul 04.
Publication Year :
2009

Abstract

Membrane protein structural biology is enjoying a steady acceleration in the rate of success. Nevertheless, numerous membrane protein targets are resistant to the traditional approach of directly crystallizing detergent solubilized and purified protein and the 'niche market' of lipidic phase crystallization is emerging as a powerful complement. These approaches, including lipidic cubic phase, lipidic sponge phase, and bicelle crystallization methods, all immerse purified membrane protein within a lipid rich matrix before crystallization. This environment is hypothesized to contribute to the protein's long-term structural stability and thereby favor crystallization. Spectacular recent successes include the high-resolution structures of the beta(2)-adrenergic G-protein-coupled receptor, the A(2A) adenosine G-protein-coupled receptor, and the mitochondrial voltage dependent anion channel. In combination with technical innovations aiming to popularize these methods, lipidic phase crystallization approaches can be expected to deliver an increasing scientific impact as the field develops.

Details

Language :
English
ISSN :
1879-033X
Volume :
19
Issue :
4
Database :
MEDLINE
Journal :
Current opinion in structural biology
Publication Type :
Academic Journal
Accession number :
19581080
Full Text :
https://doi.org/10.1016/j.sbi.2009.05.006