Using 2D crystals to analyze the structure of membrane proteins

Electron crystallography is a powerful technique for studying the structure and function of membrane proteins, not only in the ground state, but also in active conformations. When combined with high-resolution structures obtained by X-ray crystallography, electron crystallography can provide insights into the mechanism of the protein. In this chapter we discuss obtaining a three-dimensional map of membrane proteins by electron crystallography and how to combine these maps with atomic resolution models in order to study the function of membrane proteins. We argue that this approach is particularly powerful as it combines the high resolution attainable by X-ray crystallography with the visualization of the subject in the near-native environment of the membrane, by electron cryo-microscopy. This point has been illustrated by the analysis of the protein translocation complex SecYEG.