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

Revisiting limitations in time-resolved X-ray free-electron laser structures of the bacterial photosynthetic reaction center uncovers their irrelevance to proposed structural changes in electron transfer dynamics.

Building on previous work (Uervirojnangkoorn et al., 2015), we demonstrate how improved methods for processing XFEL diffraction data enable the determination of structures from poorly diffracting crystals.

Lipidated and highly hydrophobic Wnt ligands form a complex with the serum glycoprotein afamin, and can be purified and stored in a biologically active form without detergents.

Extremely short X-ray pulses from a free-electron laser are helping to clarify how phytochromes respond to light, but puzzles remain.

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.

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

Mechanical instabilities are shown to underlie the development of bacterial biofilm morphology, suggesting an ancient origin for mechano-morphogenesis, which is known to drive developmental processes in tissues in higher organisms.

CAMSAP2 co-condensates with αβ-tubulin to induce microtubule nucleation and growth, serving as a microtubule-organizing centre for non-centrosomal microtubules.

A computational model of fission yeast mitosis can interrogate mechanisms required for successful mitosis, the origin of spindle length fluctuations, and spindle force balance during assembly.