NEWS Within the framework of the UCMR Distinguished Guests Seminars Series, Professor Edward Egelman gives a hybride lecture on cryo-electron microscopy (Cryo-EM), which today has become the main technique for determining the atomic structure of macromolecules. Cryo-EM is starting to make a big impact in areas such as materials science, soft matter and chemistry.
Edward Egelman, Harrison Distinguished Professor of Biochemistry and Molecular Genetics, University of Virginia, USA
ImageUniversity of VirginiaTime: 18 October at 13-14
Venue: Stora hörsalen KBC (KBE303). Find the room
Webinarium: Please register here if you opt to join on Zoom: Registration
Lecturer: Edward Egelman, Harrison Distinguished Professor of Biochemistry and Molecular Genetics, University of Virginia, USA
Electron cryo-microscopy (cryo-EM) has emerged as the main technique for determining the atomic structure of macromolecular assemblies. Edward Egelman will discuss applications of cryo-EM to a range of polymers, including bacterial and archaeal pili, bacterial and archaeal flagella, bacterial and archaeal mating pili, extracellular cytochrome filaments that conduct electrons over long distances (“microbial nanowires”) and filamentous viruses that infect hosts living in nearly boiling acid.
Watson and Crick observed in 1956 that almost all viruses were spherical (icosahedral) or rod-like (helical) and explained this in terms of symmetry: both allowed many copies of a single protein to encapsulate a genome. The basis for spindle-shaped viruses that infect archaea has therefore been a puzzle, as they cannot be explained by either icosahedral or helical symmetry. Egelman and his research group show how they actually evolved from helical archaeal viruses, driven by the need to package a larger genome, and that these capsids can be explained by the idea of quasi-equivalence, first postulated by Caspar and Klug in 1962 with regard to icosahedral viruses.
The powerful methods that have been developed in cryo-EM of biological complexes can now be readily applied to assemblies of peptides and small molecules. Cryo-EM is thus beginning to make a real impact in areas such as materials science, soft matter and chemistry.
Edward Egelman, Ph.D. is a biophysicist known for his work on the structure and function of protein and nucleoprotein polymers. He developed the algorithm that is now widely used in cryo-electron microscopy for the three-dimensional reconstruction of helical filaments and tubes. His research has ranged from studies of actin to bacterial pili to viruses that infect hosts living in nearly boiling acid. Egelman graduated from Brandeis University in 1976 with a B.A. in physics. He started as a Ph.D. student in experimental high energy physics at Harvard, but changed fields and received his Ph.D. from Brandeis University in 1982 in biophysics. He was a Jane Coffin Childs postdoctoral fellow at the Medical Research Council Laboratory of Molecular Biology in Cambridge, UK, and became an Assistant Professor at Yale University in 1984. In 1989 he moved to the University of Minnesota where he was an Associate and Full Professor, and in 1999 moved to the University of Virginia where he is now a Harrison Distinguished Professor.
He has been president of the Biophysical Society and Editor-in-Chief of Biophysical Journal, and is a Fellow of both the Biophysical Society and the American Academy of Microbiology. In 2019 he was elected to the National Academy of Sciences of the United States.
