Crystallography reveals protein structural changes with femtosecond time-resolution.

Proteins motions can now be resolved, providing firm ground for understanding the chemical reactivity of proteins.

Detected changes on picosecond time scales are extensive in the light-sensing phytochromes, and more moderate in a photosynthetic reaction center.

The protein motions underpin the function of the proteins.

Proteins are dynamic objects and undergo conformational changes when functioning. These changes range from interconversion between states in equilibrium to ultrafast and coherent structural motions within one perturbed state. Time-resolved serial femtosecond crystallography at free-electron X-ray lasers can unravel structural changes with atomic resolution and down to femtosecond time scales. In this review, we summarize recent advances on detecting structural changes for phytochrome photosensor proteins and a bacterial photosynthetic reaction center. In the phytochrome structural changes are extensive and involve major rearrangements of many amino acids and water molecules, accompanying the regulation of its biochemical activity, whereas in the photosynthetic reaction center protein the structural changes are smaller, more localized, and are optimized to facilitate electron transfer along the chromophores. The detected structural motions underpin the proteins’ function, providing a showcase for the importance of detecting ultrafast protein structural dynamics.

© 2022 The Author(s). Published by Elsevier Ltd.