Membrane protein crystallization from lipidic phases
Journal article, 2009

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.

Author

Linda C Johansson

University of Gothenburg

Annemarie Wöhri

Chalmers, Chemical and Biological Engineering, Molecular Imaging

Gergely Katona

University of Gothenburg

Sven Engström

Chalmers, Chemical and Biological Engineering, Applied Surface Chemistry

Richard Neutze

University of Gothenburg

Current Opinion in Structural Biology

0959-440X (ISSN)

Vol. 19 4 372-378

Subject Categories

Other Chemistry Topics

DOI

10.1016/j.sbi.2009.05.006

More information

Created

10/7/2017