Structural biology has been highly successful during the last 60 years. The first protein structure of sperm whale myoglobin was solved in 1960 using X-ray crystallography, a method now producing over 10,000 structures per year, all of them deposited in and available from the Protein Data Bank (PDB). In recent years, electron cryomicroscopy (cryoEM) of single particles plunge-frozen in a thin film of amorphous ice, has developed rapidly in power and resolution, so that over 3,000 PDB depositions based on cryoEM were made in the last year. Many of these cryoEM structures represent unstable, flexible or dynamic assemblies whose structure cannot be determined by any other method, and improvements to the method are being continuously developed. We are fortunate now to have superbly detailed images of many of the most important molecules of life, with electron microscopy still having great potential to expand its reach.
Richard Henderson CH FRS FMedSci HonFRSC is a Scottish molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank.
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