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Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
Published on: September 20, 2016
Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment
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.
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