Year & Category
2017 Nobel Prize in Chemistry (jointly with Jacques Dubochet, Switzerland, and Richard Henderson, United Kingdom)
“For developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution”
At the time of the award he worked at
Columbia University, New York, USA
About his research
Cryo-electron microscopy makes it possible to image proteins and other biomolecules at atomic resolution – and visualise vital processes in three dimensions. The benefit – for example, to basic medical research – is immense. It makes it possible to carry out detailed observations of the dangerous Zika virus, for instance. Joachim Frank made a groundbreaking contribution to this imaging revolution. He was helped in this by insights he gained while working on his doctoral thesis, which he completed in 1970 at the Technical University of Munich and the Max Planck Institute of Biochemistry in Martinsried. At the time Frank was already occupied by the question of how to depict proteins in three dimensions. This form of representation is crucial for an understanding of how proteins function.
Between 1975 and 1986 Frank found a way of calculating a three-dimensional representation of the structure of a protein from a large number of two-dimensional images recorded with an electron microscope. Initially, this produced comparatively blurred images. Frank developed a mathematical method that made it possible to combine thousands of individual images of a protein using a computer to produce a high-resolution two-dimensional picture. Following another mathematical breakthrough, Frank managed to put together protein images from different perspectives in such a way that they depict a three-dimensional structure on the computer.
Based on this work, in 1990 the British scientist Richard Henderson became the first person to observe a protein at atomic resolution using an electron microscope. And in 1991 Joachim Frank used the vitrification method developed by Swiss biophysicist Jacques Dubochet to achieve an additional significant increase in resolution: vitrification freezes the water in proteins in such a way that it behaves more like glass than ice – and prevents the formation of the ice crystals that would otherwise interfere with observations. Today Joachim Frank is continuing to refine our view of the basis of life in the Frank Lab at Columbia University in New York.