Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein

Science. 2014 Dec 5;346(6214):1242-6. doi: 10.1126/science.1259357.


Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / ultrastructure*
  • Crystallography, X-Ray / methods*
  • Photoreceptors, Microbial / chemistry
  • Photoreceptors, Microbial / ultrastructure*
  • Protein Conformation
  • Time Factors


  • Bacterial Proteins
  • Photoreceptors, Microbial
  • photoactive yellow protein, Bacteria

Associated data

  • PDB/4WL9
  • PDB/4WLA