The 2017 Nobel Prize in Chemistry has been awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson ‘for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution’
Their work has allowed scientists to freeze biomolecules to look at their structures and the processes they are involved in.
According to the press release by the Nobel Prize Committee, electron microscopes were long believed to only be suitable for imaging dead matter because the powerful electron beam destroys biological material.
In 1990, Henderson succeeded in using an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This breakthrough proved the technology’s potential.
Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy two-dimensional images are analysed and merged to reveal a sharp three-dimensional structure.
Dubochet added water to electron microscopy. The water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse.
In the early 1980s, he succeeded in vitrifying water – cooling it so rapidly that it solidified in its liquid form around a biological sample, allowing the biomolecules to retain their natural shape even in a vacuum.
Following these discoveries, the electron microscope was optimised and the desired atomic resolution was reached in 2013. Researchers can now produce three-dimensional structures of biomolecules.
In the past few years, scientific literature has been filled with images of everything from proteins that cause antibiotic resistance, to the surface of the Zika virus.
‘Biochemistry is now facing an explosive development and is all set for an exciting future’, the Nobel Prize Committee said.