Former QRB Editor Richard Henderson awarded Nobel Prize We wish to celebrate our friend and editorial board colleague, and former Editor in Chief of Quarterly Reviews of Biophysics, Dr Richard Henderson, Cambridge, for being awarded the 2017 Nobel Prize in Chemistry. Richard Henderson We aim to determine the atomic structure of interesting or important membrane proteins and membrane protein complexes. We use external analysis systems which may set additional cookies to perform their analysis. This has made it possible to tackle structures that were practically impossible previously.A second problem is that X-ray or electron crystallography needs well-ordered crystals that diffract to high resolution. His interest in membrane proteins led to him working on voltage-gated sodium channels as a post-doctoral researcher at Yale University. R Henderson MRC Laboratory of Molecular Biology Francis Crick Avenue Cambridge CB2 0QH Telephone 01223 267065 Fax 01223 268305 Email …
Henderson during Nobel Prize press conference in Stockholm in 2017 Since the recent introduction of direct electron detectors and improved computer programs, the resolution of single particle electron cryomicroscopy (cryo-EM) has been greatly improved to the extent that it is now a serious alternative to crystallography. 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. In this exclusive interview for The Scientists’ Channel, watch Dr. Richard Henderson, 2017 Nobel Prize winner in chemistry, discuss the growing importance of cryo-electron microscopy for science and how leading pharmaceutical companies are working together to utilize this revolutionary technique at the newly opened Cryo-EM suite at eBIC at Diamond Light Source, Harwell Science and Innovation … There are two main problems. 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. These scientists include: After a stay in the U.S. at Yale University, New … The LMB may use cookies to analyse how you use our website. Welcome to Richard Henderson's personal/group web page in which there is a collage of some of the recent work of members of the group. We are therefore working to improve the imaging methods, the computer programs for image processing, and the efficiency of electron detectors, with the goal of realising the full potential of cryo-EM for analysis of single particle structure at atomic resolution. One of the world's leading research institutes, our scientists are working to advance understanding of biological processes at the molecular level - providing the knowledge needed to solve key problems in human health.First, many membrane proteins, including most G-protein-coupled receptors, are relatively unstable after purification in detergent: for this class of membrane proteins, Chris Tate and his colleagues in the LMB have recently developed the method of conformational stabilisation (Serrano-Vega et al (2008) PNAS, 105, 877-882) by combining a number of thermostabilising mutants to create much more stable molecules. We aim to determine the atomic structure of interesting or important membrane proteins and membrane protein complexes.
Returning to the MRC Laboratory of Molecular Biology in 1975, Henderson worked with Nigel Unwin to study the structure of the membrane protein bacteriorhodopsin by electron microscopy. These cookies (and any others in use) are detailed in our Interview: Richard Henderson, University of Cambridge | THE People A semin… Henderson was educated at Newcastleton primary school, Henderson worked on the structure and mechanism of 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.In the last few years, Henderson has returned to hands-on research focusing on single particle electron microscopy. After studies at the University of Edinburgh, he received his doctor’s degree at the University of Cambridge, MRC Laboratory of Molecular Biology, in 1969. Richard Henderson was born in Edinburgh, Scotland. The links also provide some personal information about me - a brief biographical sketch, a CV and a list of publications. [ Placeholder content for popup link ] View Richard Henderson’s profile on LinkedIn, the world's largest professional community. Richard has 6 jobs listed on their profile. This site uses cookies.