Abstract

In the last few years, single particle electron cryomicroscopy (cryoEM) has experienced a quantum leap in its capability, due to improved electron microscopes, better detectors and better software, and this is revolutionising structural biology. Using the technique invented by Jacques Dubochet and his colleagues, a thin film containing a suspension of the macromolecules of interest is plunge-frozen into liquid ethane at liquid nitrogen temperature, creating a frozen sample in which individual images of the structures can be seen in many different orientations. Subsequent computer-based image analysis is then used to determine the three-dimensional structure, frequently at near-atomic resolution. I will describe some recent results and discuss remaining barriers to progress. CryoEM is already a very powerful method, but there are still many improvements that can be made before the approach reaches its theoretical limits.