Nobel Prize awarded to Academy Fellow


Academy Fellow, Dr Richard Henderson FRS FMedSci, has been awarded the 2017 Nobel Prize in Chemistry, along with Jacques Dubochet and Joachim Frank, "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution".

Dr Richard Henderson was elected to The Academy of Medical Sciences in 1998, the founding year of the Academy. He conducts his ground breaking research at the MRC Laboratory of Molecular Biology in Cambridge.

The Academy is delighted to welcome Richard to the ranks of Fellows who are Nobel Laureates, which includes Paul Nurse, Martin Evans, John Gurdon, Venki Ramakrishnan, Sydney Brenner, Elizabeth Blackburn, Tim Hunt, Peter Doherty, Aaron Klug, John Sulston and John Walker.

Richard Henderson will receive his Nobel Prize in Sweden in December. In his reaction to the news, he said:

“I am delighted for everybody in the field that the Nobel Prize for Chemistry has been awarded to acknowledge the success of cryo-EM.  I am particularly pleased that Jacques Dubochet has been recognised as the key person who kick-started the field in the early 1980s with his method of rapid freezing to make a specimen of amorphous ice, a crucial advance.”

Richard Henderson’s Nobel Prize winning science

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

In 1990, Richard Henderson was the first to use an electron microscope to generate a three-dimensional image of a protein at atomic resolution. This was science that was previously thought to be impossible and was a major breakthrough for electron microscopy. In 2013 the desired atomic resolution was reached, a feat which would not have been possible without Richard’s work.

Because of this, researchers can now produce three-dimensional structures of biomolecules in their laboratories, changing the landscape of biochemistry. Examples of these structures include proteins that cause antibiotic resistance, and the surface of the Zika virus, allowing these molecules to be studied in great detail, fast-tracking biomedical advances.

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