Breaking the Ice: Cryo-EM's Quest for Better Resolution and Quality

Prof. Dr. Holger Stark

MPI for Multidisciplinary Sciences, Am Fassberg 11, 37077 Goettingen, Germany

E-mail: hstark1@mpinat.mpg.de

Abstract
Cryo-Electron Microscopy (cryo-EM) has become a revolutionary technique in the field of structural biology, allowing researchers to visualize biomolecular structures in ever-increasing detail. However, despite the tremendous success of cryo-EM, fundamental questions remain about the limits of achievable resolution. How far can we push the resolution limits of cryo-EM? Can we go beyond current limits and achieve atomic-level detail for more than the model protein apoferritin? Furthermore, how does resolution in cryo-EM relate to map quality? The fidelity and therefore interpretability of reconstructed maps depends on several factors, including sample quality, electron optical parameters and image processing algorithms. Understanding the relationship between resolution and map quality is essential for accurate interpretation of structural information and accurate model building. Pushing the limits of resolution and improving map quality will enable researchers to reveal finer details of molecular structures, shed light on intricate enzymatic mechanisms and pave the way for future breakthroughs in drug discovery.