Date: April 29, 2021
Time: 9:00am PDT
Cryo-electron microscopy (cryo-EM) reached single-atom resolution for 3D structure determination of biological macromolecules. Cryo-EM has been determining the structures of protein structures for soluble as well as membrane proteins that have a key role in human disease. It has become possible to obtain sufficiently high resolution structures to visualize water molecules, hydrogen atoms and in the cases of optimized samples, individual protein atoms. For protein structures, especially membrane proteins, improvements in resolution below 3 Å would mean improved rotamer assignments due to better defined side chain densities, visualization of bound drug or ligand molecules and an unambiguous assignment of structurally ordered water molecules that are very important for any structure-based drug discovery. The resolution leap is possible due to cryo-EM technological advances. We will review how our 300 kV, cryo-transmission electron microscope (Thermo Fisher Krios G4) works from the cold field emission source to detector and Selectris Imaging Filter. We will also show brand new results on membrane protein structures going beyond 2.5 Å resolution obtained with our 200kV Glacios cryo-TEM.
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