The 2017 Nobel Prize in chemistry has been awarded to three scientists who developed a technique called cryo-electron microscopy (Cryo-EM), which simplifies the process for looking at the machinery of life.
Jacques Dubochet, Joachim Frank and Richard Henderson will share the nine million kronor (£831,000) prize. Richard Hendersonis one of the renowned scientists working for the MRC Laboratory of Molecular Biology (MRC-LMB) in Cambridge, UK. The MRC-LMB has played a central role in developing the technique.
The MRC-LMB is a key collaboration partner of AstraZeneca’s IMED Biotech Unit and we will be next-door neighbours when we move into our new global HQ and research centre in Cambridge.
Cryo-EM and AstraZeneca
As early adopters of cryo-electron microscopy (Cryo-EM) and total internal reflection fluorescence (TIRF) microscopy, AstraZeneca scientists are at the forefront of single molecule science – using it to define the structure and function of large complex proteins and better understand interactions between potential new medicines and target receptors.
Cryo-EM is used by the IMED Discovery Sciences team together with several collaboration partners as part of a Cambridge area consortium of five pharma companies (AstraZeneca, GSK, UCB, Aztecs and Heptares), the MRC-LMB, the University of Cambridge, and FEI (the leading microscope company).
In collaboration with the MRC-LMB, our IMED Biotech Unit scientists have applied the technology to define the world’s first protein structures for human ataxia telangiectasia mutated (ATM). ATM is a key trigger protein in the DNA damage response and a prime therapeutic target in cancer. In a paper published in Science Advances in May this year, our scientists were able to use Cryo-EM to define the structure of ATM in different functional states. Read more on AstraZeneca.com.
In collaboration with the MRC Laboratory of Molecular Biology we have applied this technology to define the world’s first protein structures for human ataxia telangiectasia mutated (ATM). ATM is a key trigger protein in the DNA damage response and a prime therapeutic target in cancer. The LMB Cambridge are world leaders in this field and many other high impact studies have come out of this institution.
The technique makes it possible for life’s molecular building blocks to be captured mid-movement and allows scientists to visualise processes that have never before been seen. The Nobel committee said the work had “moved biochemistry into a new era”. The Nobel Prize Committee chair Sara Snogerup Linse explained: “Soon, there are no more secrets, now, we can see the intricate details of the biomolecules in every corner of our cells and every drop of our body fluids. We can understand how they are built and how they act and how they work together in large communities. We are facing a revolution in biochemistry.”
MRC-LMB, a world-renowned research institute
The work of LMB scientists has previously been recognised with the award of 10 Nobel prizes: 7 in the field of chemistry and 3 for physiology or medicine. These prizes celebrate key advances in primary scientific research and for developing pioneering techniques for molecular biology. Richard Henderson is the 15th Nobel laureate to work at the Medical Research Council (MRC) Laboratory of Molecular Biology in Cambridge.