Membrane proteins play crucial roles in many cellular processes such as signaling, nutrient uptake and cell adhesion. Although the lipid bilayer influences many aspects of membrane protein function, our understanding of lipid–protein interactions is limited. In the first part of my seminar, I will describe how electron crystallography of the water channel aquaporin-0 reconstituted with lipids into two-dimensional crystals can be used to address very basic questions in membrane biology, such as the driving forces that define lipid–protein interactions and the effects of hydrophobic mismatch. In the second part, I will discuss how we plan to use membrane proteins reconstituted into nanodiscs to make it possible to study lipid–protein interactions by single-particle cryo-electron microscopy.
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