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Recent advances in single-particle cryo-electron microscopy (cryo-EM) have enabled structure determination of small (<200 kDa) biological complexes, allowing researchers to study proteins that resist crystallization. Dr. Joost Snijder, Assistant Professor, Utrecht University, and Dr. Ieva Drulyte, Cryo-EM Application Specialist, Thermo Fisher Scientific, present the cryo-EM structure of the ~80 kDa heavily glycosylated human coronavirus HKU1 hemagglutinin esterase (HE) at a global resolution of 3.4 Å.
In this webinar, Dr. Dom Olinares discusses recent advances in single particle cryogenic electron microscopy (cryo-EM) have enabled the structural determination of numerous flexible and conformationally heterogeneous protein assemblies at high resolution, yielding unprecedented insights into their function. However, despite its extraordinary capabilities, cryo-EM remains extremely resource-intensive and time-consuming. It is therefore beneficial to have a means for rapidly assessing and optimizing the quality of samples prior to lengthy cryo-EM analyses.
Learn about integrative structural biology for viral research by watching this 10 minute video. Albert Konijnenberg, PhD, Product Manager, cryo-EM Sample Preparation & Integrative Structural Biology, Thermo Fisher Scientific, discusses the role of cryo-electron microscopy (cryo-EM) in vaccine development and as an assay for mutants. Learn how native and charge detection mass spectrometry can be used for Adeno-associated virus (AAV) particle characterization. Find out how combining structures from cryo-EM with glycan characterization by mass spectrometry can help scientists understand the bodies’ immune response to SARS-CoV-2.