Professor Grigorieff is one of the pioneers who, together with 2017 Nobel Prize in Chemistry laureate R. Henderson, laid the groundwork for structural analysis of biological molecules by cryo-electron microscopy. He has made numerous contributions to establishing high-resolution structural analysis in the field.

In this lecture, he will take us through the historical background of the field and share his latest research findings.

Date&Time: Friday, May 22, 2026, 14:00 – 15:00
Venue: Graduate School of Frontier Biosciences, Life Systems Building, 2F Seminar Room
Title: The Cryo-EM Revolution: A Story in Four Acts
Speaker: Professor Nikolaus Grigorieff
University of Massachusetts Medical School, MA, USA
Contact: Professor Takayuki Kato, tkato [at] protein.osaka-u.ac.jp（※Please replace [at] with @)

Almost fifteen years ago, single-particle electron cryo-microscopy (cryo-EM) emerged as one of the most powerful methods for determining the atomic structures of biomolecules. Today, it is a routine technique that produces high-resolution structures of molecules and molecular assemblies, rivaling those obtained by X-ray crystallography. Unlike crystallography, however, single-particle cryo-EM can visualize multiple conformational states within a single sample, offering snapshots of the functional cycles of the molecules and complexes under study.

At the same time, electron cryo-tomography (cryo-ET) is being developed to visualize molecules inside cells and tissues, revealing the three-dimensional cellular context in which they function. Despite major advances in sample preparation and image processing, cryo-ET is still typically limited to resolutions of approximately 2 nm unless averaging techniques can be applied. At this resolution, it often remains difficult to identify specific molecules and determine their functional states.

In this presentation, I will offer a brief historical perspective on cryo-EM’s rise to prominence, discuss the strengths and current limitations of cryo-ET, and introduce 2D template matching, a new technique for placing molecules of known structure precisely into cellular environments.