Holger Stark
Researcher
Max-Planck-Institute for Multidisciplinary Sciences
Date and time: February 4th, 2026 Wednesday at 8am PST / 11am EST / 4pm GMT / 5pm CET / 12am China
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Is Cryo-EM as Good as It Gets? Where We Stand, What We’re Missing, and Why It Matters.
Single-particle cryo-electron microscopy (cryo-EM) has become a transformative technique for determining the three-dimensional structures of biomolecules, building on nearly a century of innovation since the invention of the electron microscope in the early 1930s. Over the past decade, advances in microscope hardware, computational power, and image-processing algorithms have enabled atomic-level structure determination of proteins and large macromolecular complexes. During this time, cryo-EM has resolved many challenging structural biology targets that previously eluded X-ray crystallography.
The rapid expansion of high-end microscopes, powerful computing resources, and user-friendly software has propelled cryo-EM to even rival X-ray crystallography in the annual number of structure depositions. Yet, despite this remarkable progress, significant technical bottlenecks and limitations remain. At a time when cryo-EM seems to have reached maturity as a structural biology method, it is crucial to take a closer look at its current constraints and identify where future improvements are most needed.
This presentation will examine these challenges and explore strategies to further enhance the resolution, quality, and throughput of cryo-EM