Electron crystallography as a technique to study the structure on membrane proteins in a lipidic environment.
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.
Max Planck Institute of Molecular Physiology, 44227 Dortmund, Germany. stefan.raunser@mpi-dortmund.mpg.de
Stefan
S
Raunser
Thomas
T
Walz
D003461:Crystallography / Q000379:methods*; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure*; D008854:Microscopy, Electron / Q000379:methods*; D011487:Protein Conformation
D008051:Lipid Bilayers; D008565:Membrane Proteins