Oral Presentation The 43rd Lorne Conference on Protein Structure and Function 2018

The increasing power of cryoEM for macromolecular structure determination. (#13)

Richard Henderson 1
  1. MRC Laboratory of Molecular Biology, Cambridge, CAMBRIDGESHIRE, United Kingdom

In the last few years, single particle electron cryo-microscopy (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-hydrated 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 show examples of some recent structures, 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. I will also include some historical perspective on how I became an electron cryomicroscopist.