Recognizing that interaction with the air–water interface (AWI) is a major challenge for cryo-
EM, we first review current approaches designed to avoid it. Of these, immobilizing particles …

All steps of cryogenic electron-microscopy (cryo-EM) workflows have rapidly evolved over
the last decade. Advances in both single-particle analysis (SPA) cryo-EM and cryo-electron …

Single particle cryo-EM often yields multiple protein conformations within a single dataset,
but experimentally deducing the temporal relationship of these conformers within a …

Careful selection of photocaging approaches is critical to achieve fast and well synchronized
reaction initiation and perform successful time-resolved structural biology experiments. This …

Molecular machines, such as polymerases, ribosomes, or proteasomes, fulfill complex tasks
requiring the thermal energy of their environment. They achieve this by restricting random …

The structural determination of biological macromolecules has been transformative for
understanding biochemical mechanisms and developing therapeutics. However, the …

G-protein-coupled receptors (GPCRs) activate heterotrimeric G proteins by stimulating
guanine nucleotide exchange in the Gα subunit. To visualize this mechanism, we developed …

The α7 nicotinic acetylcholine receptor is a pentameric ligand-gated ion channel that plays
an important role in cholinergic signaling throughout the nervous system. Its unique …

Developments within the cryo-EM field have allowed us to generate higher-resolution “static”
structures and pull out different conformational states which exist at equilibrium within the …

Cryo-electron microscopy (CryoEM) has superseded X-ray crystallography and NMR to
emerge as a popular and effective tool for structure determination in recent times. It has …