Serial femtosecond crystallography reveals protein dynamics in real time
By 
Clare Sansom2025-07-21T08:50:00
Proteins are constantly moving, but our structures of them are static. Clare Sansom talks to the researchers using free-electron lasers to make time-resolved structures
Until fairly recently, everything we understood about the structure of proteins and other biological macromolecules was derived from static images. Each of the almost 200,000 x-ray crystal structure entries in the Protein Data Bank (PDB) is an atomic model of a protein or other macromolecule refined to fit experimental data. It is easy to imagine that structure as distinct and apparently unmoving. However, if you were, in a thought experiment, to shrink yourself down to protein level and look inside a living cell, everything you would see would be in constant motion.
It has taken a step change in the methodology of x-ray crystallography possibly equivalent to the birth of film from still photography to make it possible to deduce function from molecular movements across a time series of ‘stop-motion’ atomic models progressing along a reaction coordinate.