Cambridge MRC LMB biologist Richard Henderson one of Nobel Prize in Chemistry winners

PUBLISHED: 11:49 04 October 2017 | UPDATED: 14:32 04 October 2017

Richard Henderson © Nobel Media. Ill. N. Elmehed

Richard Henderson © Nobel Media. Ill. N. Elmehed

ILIFFE

The Darwin College Fellow has worked at the MRC Laboratory of Molecular Biology in Cambridge since 1973.

The Nobel Prize in Chemistry 2017 was awarded to MMRC Laboratory of Molecular Biology scientist Richard Henderson, Jacques Dubochet and Joachim Frank “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution”.

The scientists simplified and improved imaging of biomolecules and the Nobel Foundation says the method they developed moved biochemistry into a new era.

In 1990, Richard Henderson, who began studies for a Ph.D. at Cambridge University in 1966, 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.

:: Cambridge alumni win 2016 Nobel Prize in Physics

Electron microscopes were long believed to only be suitable for imaging dead matter, because the powerful electron beam destroys biological material.

Joachim Frank made the technology generally applicable. Between 1975 and 1986 he developed an image processing method in which the electron microscope’s fuzzy twodimensional images are analysed and merged to reveal a sharp three-dimensional structure.

:: How Cambridge scientists are exploring the incredible transport system inside our cells

Jacques 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.

The desired atomic resolution was reached in 2013, and researchers can now routinely produce three-dimensional structures of biomolecules.

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