Table 2 FEL X-ray data collection properties and their anticipated impact on the delivery of structural information to facilitate structure-based drug discovery
Property of XFELImpact to structure-based drug discovery
Unprecedented peak brilliance and μ-focus beam (~0.2–1.5 μm)Better resolution of the structural information, work with smaller crystals (<1 μm), shortening of crystallization optimization time
Femtosecond X-ray pulsesEnabling fs time-esolved measurements, observation of intermediate structural changes upon ligand binding, changes in water structure upon ligand binding
Low/no radiation damageRadiation sensitive groups (metal complexes) are kept in physiological conditions
Properties of serial crystallography at XFEL (SFX) and synchrotron (SMX)
Room temperatureNo freezing protocol required with risk of crystal deterioration, more physiological, more realistic information on dynamic and conformation of structures
Full automation of data collectionFull liquid handling procedure, no crystal mounting
Data redundancyEfficient screening of thousands of crystals, improved structure quality, native sulphur phasing
  • The XFEL triggered development in serial crystallography benefits both, synchrotron and XFEL data recording.