Cryo-electron microscopy wins the 2017 chemistry Nobel Prize

On October 4, 2017, Jacques Dubochet (Switzerland), Joachim Frank (USA) and Richard Henderson (UK) were awarded the chemistry Nobel Prize for cryo-electron microscopy (Cryo-EM).

The three researchers contributed to developing a technique that allows scientists to see the intricate structures of proteins, nucleic acids and other biomolecules, and even study how they move and change as they perform their functions. It is a useful technology to understand how the way biomolecules function and interact is fundamental to biochemistry, and underpins efforts to develop new drugs and medical treatments, and understand and treat diseases.

Richard Henderson was the first person to generate an image of a protein using transmission electron microscope (TEM). TEMs use a beam of electrons to examine the structure of molecules and materials at the atomic scale. However, this technology does not allow to visualize some materials such as biomolecules. The water that surrounds the molecules evaporates, and the high energy electrons burn and destroy the molecules. Cryo-EM uses frozen samples, gentler electron beams and sophisticated image processing to overcome these problems.

Joachim Frank’s contributed to the field by processing and analysing cryo-EM images. James Dubochet developed the method for freezing water-based TEM samples so rapidly that the water forms a disordered glass, rather than crystalline ice.

Recently, this kind of technology has been used to generate a high-resolution 3D image of the Zirka virus structure. It provided a starting point for searching for possible sites that could be targeted by drugs to prevent the spread of the virus.

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