Dubochet, Frank share the joy of Nobel chemistry win

Oct 06, 2017, 00:21
Dubochet, Frank share the joy of Nobel chemistry win

The Royal Swedish Academy of Sciences has produced an easy-to-read history about the role each of the three winners played in the development of cryo-electron microscopy; there is also an 18-page scientific summary of the research. Using it, scientists have made high-resolution, 3D images to target cancer drugs and demystify the Zika virus. Between 1975 and 1986, Frank developed a new method to process electron microscopes' images into a more sharp, 3D structure.

The method is called cryo-electron microscopy.

For many years - in the 1970s, the electron microscope was the only way to look into the cell and observe the minute beings that play such an important role in our lives such as viruses. Dubochet, a biophysicist at the University of Lausanne in Switzerland, advanced electron microscopy toward cryo-EM in the 1980s, when he applied a vitrification technique to samples, allowing them to be rapidly frozen in a way that would not allow water to disturb the electron beams used to create the images.

Born in Scotland in 1945, Henderson did a BSc in physics at the University of Edinburgh before completing a PhD in molecular biology at the University of Cambridge, UK, in 1969.

Historically, TEM also presented difficulties.

Applying electron microscopy to biology was a challenge because the technique is done in a vacuum, which can dry out and distort the shape of proteins and other biological molecules. Due to their work, electron microscopes are now able to visualise proteins at atomic resolution. It was a breakthrough moment. Finally, in 1990, 15 years after he had published the first model, Prof.

It's been hard to capture life's "molecular machinery", however, meaning we don't really know what the 3-D structure of biomolecules looks like, which hampers our ability to understand them.

Dubochet came up with a sophisticated approach to prevent molecules from drying out. X-ray crystallography required well-organised crystals - biomolecules are usually never organised as crystals. Conventional freezing doesn't help: Ice crystals rupture cell membranes and push the proteins around; the biomolecules react faster than the water freezes; and evaporating ice crystals disrupt the fidelity of the images. And we can understand how a hormone like oestrogen or testosterone binds to something then goes down and touches the complexes that regulate gene expression, and how that leads to responses. He later worked at several universities and research labs worldwide before joining Columbia University as professor of biochemistry and molecular biophysics and of biological sciences in 2008.

Among the processes it has made clearer is the mechanism by which DNA is copied into the single-stranded molecule RNA. 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.

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