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Annu Rev Biophys. 2009;38:89-105. doi: 10.1146/annurev.biophys.050708.133649.

Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment.

Author information

  • 1Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany. stefan.raunser@mpi-dortmund.mpg.de

Abstract

The native environment of integral membrane proteins is a lipid bilayer. The structure of a membrane protein is thus ideally studied in a lipidic environment. In the first part of this review we describe some membrane protein structures that revealed the surrounding lipids and provide a brief overview of the techniques that can be used to study membrane proteins in a lipidic environment. In the second part of this review we focus on electron crystallography of two-dimensional crystals as potentially the most suitable technique for such studies. We describe the individual steps involved in the electron crystallographic determination of a membrane protein structure and discuss current challenges that need to be overcome to transform electron crystallography into a technique that can be routinely used to analyze the structure of membrane proteins embedded in a lipid bilayer.

PMID:
19416061
[PubMed - indexed for MEDLINE]
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