A new electron diffraction technique called MicroED allows protein structures to be determined from three-dimensional microcrystals.

Building on previous work (Shi et al., 2013), we have used MicroED to determine the structure of catalase at 3.2 Å resolution from a single crystal.

Time-resolved serial femtosecond crystallography revealed retinal kink and early changes in channelrhodopsin, which leads to the ion pore formation.

Time-resolved crystallography provides insight into the photochemical reactions in photoreceptor proteins, explaining the earliest steps of how plants, fungi and bacteria sense red light.

Aqueous solubility of cystic fibrosis drug ivacaftor is ~200-fold lower, whereas the potency of its stimulatory effect on the CFTR channel is >100-fold higher, than reported, and is fully reversible.

The structures of photosystem II, with the water-oxidizing Mn4CaO5-cluster fully removed and in an intermediate assembly state, show that photoassembly is facilitated by perfectly pre-arranged protein ligands of the five metal ions.

Solid state NMR is unable to detect any association of substrate to the second binding site, S2, in the extracellular vestibule of the Neurotransmitter:Sodium Symporter LeuT.

A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

Atomic structures of hIAPP fibrillar segments, determined using the cryo electron microscopy method MicroED, reveal that strong, stable intermolecular interactions are important features of cytotoxic amyloid proteins.

The earliest fossil evidence of a mimetic relationship between the Jurassic moth lacewing Lichenipolystoechotes and its co-occurring fossil lichen Daohugouthallus predates modern lichen-insect associations by 165 million years.