Understanding Biological Machinery by Cryogenic TEM
Friday, January 26, 2018 at 1 PM Eastern Time
Dr. Williams is an Associate Research Scientist at Arizona State University, where he is establishing a regional cryogenic TEM facility for near-atomic resolution imaging of macromolecular assemblies of cellular components. His primary interface is facilitating user success in sample preparation, imaging, and 3D image reconstruction. The cryoTEM facility is housed within Arizona State Universities Office of Knowledge and Enterprise Developments’ Material Characterization and Synthesis core, historically known as the Leroy Eyring Center for Solid State Science. Dr. Williams previously was the Director of EM resources at the University of Pennsylvania Medical Center and was a member of the Biochemistry and Biophysics Department.
Dr. Katia March is an Associate Research Scientist at the Arizona State University Material Characterization and Synthesis core facility. For the last year she has been in charge, of the first delivered NION monochromated scanning electron microscope. Previously she was a CNRS Research Engineer in the Electron Microscopy group in Orsay (France) under the direction of Christian Colliex and Odile Stéphan. Her main fields of interest are the development of new instrumentation and experimental methods relying on electron energy loss spectroscopy (EELS). The Nion microscope is a unique tool for materials science investigations which has made it possible to record optical and IR spectra at the nanoscale level (vibrational modes, optical excitations from defects). Her main duties are helping users design experiments that achieve their scientific objectives while pushing the limits of electron microscopy at very high energy resolution.
Life is composed of four fundamental building blocks: lipids, sugars, nucleic acids, and amino acids. These basic building blocks polymerize and assembly into the living world around us. Historically, understanding how this organic chemistry creates the machinery of life required crystallization and x-ray diffraction methods, or were limited to sizes solvable by NMR spectroscopy. Today, advances in cryogenically preserving biological assemblies and imaging them by Transmission Electron Microscopy are revolutionizing our understanding of these molecular assemblies in near native conditions with spatial resolutions ranging from organismal to near atomic resolutions. This webinar will discuss these advances and why the researchers behind them were recently awarded the Nobel Prize in Chemistry.