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.

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.

Structures of multiple states of two dicarboxylate transporters explain the conformational changes needed for substrate import.

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

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

A comprehensive structural analysis of inhibitory murine antibody 3D11 binding to Plasmodium berghei circumsporozoite protein reveals common mechanisms of antibody evolution in mammals against Plasmodium parasites.

Structural and biochemical analysis of the mechanism of paroxetine binding to the serotonin transporter provides a framework for transporter inhibition and design of small-molecule inhibitors.

X-ray phase-contrast tomography reveals pathology of capillaries in heart tissue from patients who succumbed to Covid-19, as well as alterations in the three-dimensional cardiac tissue structure.

The structure of a voltage-activated potassium channel in lipid nanodiscs solved using cryo-electron microscopy is similar to previous X-ray structures, and provides insights into the mechanism of C-type inactivation.