The Nobel Prize in Chemistry has been awarded to Jacques Dubochet, Joachim Frank and Richard Henderson for the development of cryo-electron microscopy, which both simplifies and improves the imaging of biomolecules.
They won the prize for “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution”, the Royal Swedish Academy of Sciences said while announcing the award here on Wednesday.
“This method has moved biochemistry into a new era,” the Academy said.
The works of Dubochet, affiliated with University of Lausanne in Switzerland, Frank with Columbia University in New York and Henderson with MRC Laboratory of Molecular Biology in Britain paved the way for imaging 3D structures of biomolecules.
Electron microscopes were long believed to only be suitable for imaging dead matter because the powerful electron beam destroys biological material.
But 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. Liquid water evaporates in the electron microscope’s vacuum, which makes the biomolecules collapse.
In the early 1980s, Dubochet succeeded in vitrifying water — he cooled water 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’s every nut and bolt have been optimised.
The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules.