iThe three-dimensional structure of proteins is decisive for their biological function. For a long time, X-ray structure analysis was the means of choice to determine this structure with atomic resolution. But often proteins could not be crystallized. Moreover, in many cases, the shape of the protein changes in the course of the reaction - which can not be represented by a static crystal structure.
With the cryo-electron microscopy, Jacques Dubochet, Joachim Frank and Richard Henderson have created a tool helping to bridge this gap. Using liquid nitrogen, the sample is cooled in the microscope reducing the destructive influence of the electron beam. In addition, the water contained in the sample is retained by extremely fast cooling.
In continuation of the work of his doctoral advisor Hoppe, Joachim Frank succeeded in developing a strategy that can calculate a three-dimensional image of the structure from a large number of two-dimensional high-resolution images of an electron microscope.
At the Technical University of Munich, too, cryo-electron microscopy is currently used for the elucidation of the structure and function of proteins, additional to X-ray structure analysis and NMR spectroscopy.
"I am delighted that these three researchers are honored with the Nobel Prize," says Sevil Weinkauf, Professor of Electron Microscopy at the TU Munich. "They are the pioneers in this field, and behind them are even more researchers with important contributions to bringing this method a major leap forward over the last few years."
Up to now (2017), 17 scientists and alumni from the Technical University of Munich (TUM) were awarded with a Nobel Prize.