The M&M 2019 Executive Program Committee is very pleased to present two of the three 2017 Laureates of the Nobel Prize in Chemistry "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution" and shared with Jacques Dubochet.
Joachim Frank, Ph.D.
Professor of Biochemistry, Molecular Biophysics, and Biological Sciences, Columbia University
Studying Kinetics by Counting Particles in Time-Resolved Cryo-EM
Dr. Joachim Frank's major contribution to the field has been in developing mathematical and computational methods for processing and analyzing cryo-EM images of multiple randomly-oriented molecules within a sample and compiling them into a representative 3D structure.
Dr. Frank used his algorithms to generate the first 3D images of the ribosome - a large structure made of several proteins and RNA strands, which is responsible for translating RNA into proteins inside cells in all organisms. With this distinctive technique, when combined with Dubochet's method of ice-embedding, information on conformational changes of macromolecules in their native states can be obtained, which enables a deeper understanding of the way 'molecular machines' function in cells. Structures of many molecules that resist crystallization and hence cannot be studied by X-ray crystallography can now be elucidated. Initially, the resolution that could be obtained was limited by the poor performance of recording media. This technical problem was solved 7 years ago with the introduction of cameras capable of detecting single electrons. The development of cryo-electron microscopy has revolutionized the imaging of biomolecules and propelled biochemistry into a new era. By now, about 1500 structures of proteins and RNA-protein complexes have been solved and entered in a public database, making this knowledge a fast growing and increasingly important contribution to molecular medicine and the development of drug therapies.
Dr. Frank's achievements were recognized with MSA's Distinguished Biological Scientist award in 2003, and he was named an MSA Fellow in 2009.
Richard Henderson, Ph.D.
Professor of Biochemistry, Medical Research Council Laboratory of Molecular Biology (MRC LMB) - Cambridge, United Kingdom
Single-Particle CryoEM: Potential for Further Improvement
Dr. Richard Henderson developed TEM into a tool for the direct determination of the structure of proteins, and applied it most notably to two-dimensional (2D) crystals of the purple light-harvesting protein, bacteriorhodopsin. Images and electron diffraction patterns of many 2D crystals of bacteriorhodopsin from multiple angles were acquired using low-dose electron exposures, and combined to generate a 3D image of the protein. He continued to refine this technique over many years until he produced images at similar resolutions as those from X-ray diffraction. Later, Dr. Henderson turned his attention to the development and improvement of methods of high-resolution electron cryo-microscopy and single particle structure determination. With colleagues, he advanced these techniques for exploring high resolution ultrastructure of membrane proteins, protein complexes and other non-crystalline biomolecules in solution. During this journey, Dr. Henderson made critical contributions to many of the single particle electron microscopy approaches, including pioneering the development of direct electron detectors.
Dr. Richard Henderson was presented with MSA's Distinguished Biological Scientist award in 2005, and was named as an MSA Fellow in 2009.