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 The XFEL, first used in this century, has ultrahigh intensity and ultrashort pulse characteristics and enabled the observation of biomacromolecular structures before the onset of radiation damage. Furthermore, it enables high spatial and temporal resolution observation of structural changes and chemical interactions in a biomacromolecule. At SACLA (SPring-8 Angstrom Compact Free Electron Laser), we work on developing measurement methodologies and acquiring dynamic structures of biomacromolecules such as proteins captured by XFEL.
 We measure with serial femtosecond crystallography (SFX), a crystal structure determination method using XFEL, and focus on developing techniques for time-resolved experiments combining SFX with a reaction initiation trigger like photoexcitation. Conventional methods made it difficult to view molecular movements at an atomic level on a large time scale; however, time-resolved SFX allows us to visualize how molecules function as a movie at the atomic level. Insights from the dynamic structures obtained by time-resolved SFX will contribute to the deepening of life science research and aid in the design and development of new functional molecules.

X-ray Free Electron Laser “SACLA”


Making molecular movies 〜Time-resolved serial femtosecond Crystallography〜


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