Cool way to peer into molecules' inner workings wins chemistry Nobel Prize

Nobel prize in chemistry 2017 winners

The method - which "moved biochemistry into a new era", according to the Royal Swedish Academy of Sciences - works by freezing biomolecules mid-movement in order to visualize many processes that were otherwise unseen by science.

During the same decade, Frank, of Columbia University in NY, and his colleagues developed image-processing software to make sense of the fuzzy images that are produced when an electron microscope is aimed at a protein, and to convert these two-dimensional blurs into 3D molecular structures. This causes surrounding water to evaporate, and the molecules being studied collapse and lose their normal structure.

These and other improvements enabled Henderson to create the first atomic resolution of images of a protein using cryo-EM in 1990.

Cryo-electron microscopy was first developed in the 1980s as a means of imaging biological specimens without their delicate tissues being damaged by the process of electron microscopy, which had previously been limited to non-living subjects.

Practical applications of the technique are "immense", Frank told journalists after the Prize's announcement.

Because the powerful electron beam destroys biological material, electron microscopes were long believed to work only when imaging dead matter.

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Joachim Frank's strategy built upon having a computer discriminate between the traces of randomly positioned proteins and their background in a fuzzy electron microscope image. The introduction of Direct Electron Detectors in electron microscopes in 2012-13 turned out to be a powerful tool for scientists as they encountered the challenge of the Zika virus that spread rapidly across various countries in 2015-16.

Dubochet earned a doctoral degree in 1973 at the University of Geneva and University of Basel and became an honorary professor of biophysics at the University of Lausanne, Switzerland.

John Hardy, professor of neuroscience at University College London, described the development of cryo-electron microscopy as "transformative".

From 1901 to 2016 was awarded to 108 Nobel prize in chemistry.

It has laid bare never-before-seen details of the machinery inside cells, viruses and proteins, and has shed light on enzymes involved in diseases such as Alzheimer's. As electron microscopes have improved over the intervening years (in part thanks to Henderson's efforts) cryo-electron microscopy can now image biological molecules at the atomic level. "Knowing this structure opens up the possibility of rational drug design in this area". The Royal Swedish Academy has already awarded prizes in physics and medicine.

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