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

Post-refinement methods enable the use of X-ray free electron lasers for biological crystallography of systems in which sample quantity is a limitation.

Electron crystallography and molecular dynamics simulations show that a cholesterol sandwiched in between two neighboring aquaporin-0 tetramers stabilizes the association between the tetramers and thus promotes array formation.

Sodium ions but not protons induce defined helix movements in a sodium/proton antiporter and suggest a mechanism for Na + binding and transport.

The transmembrane shape of the F₁F_o ATP synthase monomer provides the molecular basis of high curvature at the ridges of mammalian mitochondrial cristae.

The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

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

The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.

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.