Speaker
Description
Understanding biological function at the molecular level requires direct visualization of macromolecular structure. For decades, structural biology has relied on approaches such as X ray crystallography and nuclear magnetic resonance spectroscopy. Over the past decade, cryo electron microscopy has rapidly matured into a central method for protein structure determination, expanding the scope of questions that can be addressed at high resolution. In 2025, over 10,000 structures were deposited into the electron microscopy data bank, and in the next few years it is projected single particle cryoEM will become the predominant technique for protein structure determination.
Cryo electron microscopy enables structure determination of proteins and macromolecular complexes in a near native, vitrified state without the need for crystallization. In particular, single particle analysis has become a powerful and widely adopted method for high resolution structure determination of soluble proteins, membrane proteins, viral particles, and dynamic multicomponent assemblies. Advances in direct electron detectors, electron optics, automation, and computational image processing now make near atomic resolution structure determination increasingly routine in many academic laboratories.
The impact of cryo EM extends across diverse areas of the life sciences. In virology and infectious disease research, cryo EM has resolved the structures of viral surface proteins, intact virions, and host pathogen complexes, directly informing vaccine design and antiviral development. In therapeutic research, from small molecules to biologics and monoclonal antibodies, cryo EM enables detailed visualization of ligand binding, antigen antibody interactions, and epitope mapping, accelerating structure guided drug design. In plant biotechnology and crop science, structural insights into photosynthetic complexes, stress response machinery, and plant pathogen interactions are guiding strategies to improve yield, resilience, and food security.
At the same time, advances in in silico protein structure prediction, including AI based approaches such as AlphaFold, have transformed computational modelling. While these tools are powerful, experimental structural biology remains essential. Cryo EM provides direct structural validation, captures conformational heterogeneity, reveals ligand binding and complex formation, and enables the study of assemblies and cellular environments that remain difficult to access computationally.
This presentation will introduce the fundamental principles of cryo EM and single particle analysis, placing the method within the broader structural biology workflow. Key steps, including sample preparation, vitrification, data acquisition, and image reconstruction, will be outlined with emphasis on practical considerations. Examples from modern 200 kV cryo TEM platforms such as the Glacios microscope will illustrate how recent technological developments support a wide range of research projects.
The talk will conclude by looking beyond isolated particles toward cryo electron tomography and in situ structural analysis. These approaches enable visualization of molecular machines directly within cells, bridging molecular and cellular scales and opening new opportunities to study biology in its native context.
