Cryogenic electron microscopy (cryo-EM) enables structure determination of
macromolecular objects and their assemblies. Although the techniques have been …

Background Since the introduction of what became today's standard for cryo-embedding of
biological macromolecules at native conditions more than 30 years ago, techniques and …

Macromolecular complexes that exhibit continuous forms of structural flexibility pose a
challenge for many existing tools in cryo-EM single-particle analysis. We describe a new …

The new developments in Cryo-EM Single Particle Analysis are helping us to understand
how the macromolecular structure and function meet to drive biological processes. By …

Cryo-electron microscopy (cryo-EM) is an imaging modality that provides unique insights
into the dynamics of proteins and other building blocks of life. The algorithmic challenge of …

Single-particle cryo-electron microscopy (cryo-EM) is a technique that takes projection
images of biomolecules frozen at cryogenic temperatures. A major advantage of this …

Macromolecules change their shape (conformation) in the process of carrying out their
functions. The imaging by cryo-electron microscopy of rapidly-frozen, individual copies of …

Image processing in cryogenic electron tomography (cryoET) is currently at a similar state as
Single Particle Analysis (SPA) in cryogenic electron microscopy (cryoEM) was a few years …

This article presents an original approach for extracting atomic-resolution landscapes of
continuous conformational variability of biomolecular complexes from cryo electron …

Cryo electron tomography (cryo-ET) allows observing macromolecular complexes in their
native environment. The common routine of subtomogram averaging (STA) allows obtaining …