Richard Henderson | |
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.jpg) Henderson during Nobel Prize press conference in Stockholm in 2017 | |
| Born | (1945-07-19)19 July 1945 (age 80) Edinburgh, Scotland |
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| Known for | Cryo-electron microscopy[2] |
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| Scientific career | |
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| Thesis | X-Ray Analysis of α-chymotrysin: Substrate and Inhibitor Binding (1970) |
| Doctoral advisor | David Mervyn Blow |
Richard Henderson is a British molecular biologist and biophysicist and pioneer in the field ofelectron microscopy ofbiological molecules. Henderson shared theNobel Prize in Chemistry in 2017 withJacques Dubochet andJoachim Frank.[3] "Thanks to his work, we can look at individual atoms of living nature, thanks to cryo-electron microscopes we can see details without destroying samples, and for this he won the Nobel Prize in Chemistry."[4]
Henderson was educated at Newcastleton primary school,Hawick High School andBoroughmuir High School.[5] His father was a baker.[6] He went on to study Physics at theUniversity of Edinburgh graduating with aBSc degree in Physics, 1st Class honours in 1966.[5] He then commenced postgraduate study atCorpus Christi College, Cambridge,[7] and obtained hisPhD degree from theUniversity of Cambridge in 1969.[5][8]
Henderson worked on the structure and mechanism ofchymotrypsin for his doctorate under the supervision ofDavid Mervyn Blow at theMRC Laboratory of Molecular Biology.[9] His interest inmembrane proteins led to him working on voltage-gatedsodium channels as a post-doctoral researcher atYale University. Returning to theMRC Laboratory of Molecular Biology in 1975, Henderson worked withNigel Unwin to study the structure of themembrane proteinbacteriorhodopsin byelectron microscopy. A seminal paper inNature by Henderson and Unwin (1975)[10] established a low resolution structural model for bacteriorhodopsin showing the protein to consist of seven transmembrane helices. This paper was important for a number of reasons, not the least of which was that it showed that membrane proteins had well defined structures and that transmembrane alpha-helices could occur. After 1975 Henderson continued to work on the structure ofbacteriorhodopsin withoutUnwin. In 1990 Henderson published an atomic model ofbacteriorhodopsin by electron crystallography in theJournal of Molecular Biology.[11] This model was the second ever atomic model of a membrane protein. The techniques Henderson developed for electron crystallography are still in use.
Together with Chris Tate, Henderson helped develop conformational thermostabilisation: a method that allows any protein to be made more stable while still holding a chosen conformation of interest.[12][failed verification] This method has been critical in crystallising and solving the structures of severalG protein–coupled receptors (GPCRs).[13] With help from the charityLifeArc, Henderson and Tate founded theMRC start-up company, Heptares Therapeutics Ltd (HTL) in 2007.[14] HTL continues to develop new drugs targeting medically important GPCRs linked to a wide range of human diseases.[9]
In the last few years, Henderson has returned to hands-on research focusing on single particle electron microscopy. Having been an early proponent of the idea that single particle electron microscopy is capable of determining atomic resolution models for proteins, explained in a 1995 paper in Quarterly Reviews of Biophysics. Henderson aims to be able to routinely obtain atomic structures without crystals. He has made seminal contributions to many of the approaches used in single particle electron microscopy, including pioneering the development of direct electron detectors that recently allowed single particle cryo-electron microscopy to achieve its goals.[3]
Although Henderson has typically worked independently, he has trained a number of scientists who have gone on to independent research careers. These scientists include:
Henderson has worked at theMedical Research CouncilLaboratory of Molecular Biology (MRC LMB) inCambridge since 1973, and was its director between 1996 and 2006.[16] He was also a visiting professor at the Miller Institute of theUniversity of California, Berkeley in Spring 1993.[17] He is currently[when?] a mentor for theAcademy of Medical Sciences Mentoring Scheme.[9] Outside academia, he lists his interests as hill walking in Scotland, kayaking and drinking good wine.[5][9]
He was interviewed byJim Al-Khalili forThe Life Scientific, first broadcast onBBC Radio 4 in February 2018.[2]
including the Nobel Lecture on 8 December 2017From Electron Crystallography to Single Particle cryoEM| Key concepts |
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