M J Thirumalachar & M J Narasimhan Memorial Lecture Dr. Richard Henderson

Location: Faculty Hall


Cordially Invites  you  to the

Dr. Richard Henderson
Nobel Laureate 2017 Chemistry
MRC Laboratory of Molecular Biology
Cambridge, UK
The cryoEM revolution in structural biology

In the last few years, single particle electron cryo-microscopy (cryoEM) has experienced a quantum leap in its capability, due to improved electron microscopes, better detectors and better software, and this is revolutionizing structural biology.  Using the technique invented by Jacques Dubochet and his colleagues, a thin film containing a suspension of the macromolecules of interest is plunge-frozen into liquid ethane at liquid nitrogen temperature, creating a frozen-hydrated sample in which individual images of the structures can be seen in many different orientations.  Subsequent computer-based image analysis is then used to determine the three-dimensional structure, frequently at near-atomic resolution. I will show examples of some recent structures, and discuss remaining barriers to progress.  CryoEM is already a very powerful method, but there are still many improvements that can be made before the approach  reaches its theoretical limits.

About the Speaker

Dr. Richard Henderson was originally a physicist from Edinburgh University but switched into molecular biology at age 21. He went as a research student to the MRC Laboratory of Molecular Biology (LMB) in Cambridge, UK where he joined the team led by David Blow that worked out the atomic structure of the enzyme chymotrypsin, one of the first few protein structures to be determined using X-ray crystallography. He went on as a Helen Hay Whitney postdoctoral fellow at Yale University to develop an interest in the structure of membrane proteins, working for a few years on voltage dependent ion channels. After returning to LMB in 1973, he began to collaborate with Nigel Unwin and together they developed electron microscopy into a tool for the direct determination of the structure of proteins, and applied it most notably to the light-driven proton pump, bacteriorhodopsin, from Halobacteria. During the next 15 years, he worked to solve a number of the technical and conceptual problems which limited the attainable resolution of electron crystallography and by 1990, he and his colleagues had succeeded in obtaining the first atomic structure of the membrane protein, bacteriorhodopsin, by using electron microscopy and diffraction. Subsequent analysis of the structure of some of its photochemical intermediates has helped to understand how bacteriorhodopsin and other closely related family members function. Now he has turned his attention to single particle electron microscopy where more advanced electron cryomicroscopy offers the promise of being able to determine atomic structures of large protein assemblies without the need first to make crystals. These methods are now being used to solve many of the outstanding problems in structural biology.

He was Joint-Head of the Division of Structural Studies at the MRC Laboratory of Molecular Biology from 1986 until 2001, and has been Director from 1996 to 2006.  He is a fellow of the Royal Society and a Foreign Associate of the US National Academy of Sciences.

*(Copied from Dr. Richard’s biographical note


Date :  Tuesday, the 23rd  January, 2018
Time :   11.00 am to 12.00 Noon
Prof. Anurag Kumar, Director –    will preside