Single particle electron cryomicroscopy (CryoEM) has experienced a surge in its capability in recent years, due to improved microscopes, better detectors and better software. This has transformed the method into a powerful technique for structure determination of biological assemblies. For many specimens, it is now more powerful than X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy (NMR). It can be carried out with smaller amounts of material that is less pure and less stable, and can be used to resolve multiple states with a small amount of extra effort. I will show examples of recent structures, and discuss some remaining barriers to further progress. CryoEM is already a very powerful method, but there are many improvements that can be made before the approach reaches its theoretical limits.