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Article Dans Une Revue Acta crystallographica Section D : Structural biology [1993-...] Année : 2024

From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons

Résumé

Over the last decade, the development of time-resolved serial crystallography (TR-SX) at X-ray free-electron lasers (XFELs) and synchrotrons has allowed researchers to study phenomena occurring in proteins on the femtosecond-to-minute timescale, taking advantage of many technical and methodological breakthroughs. Protein crystals of various sizes are presented to the X-ray beam in either a static or a moving medium. Photoactive proteins were naturally the initial systems to be studied in TR-SX experiments using pump–probe schemes, where the pump is a pulse of visible light. Other reaction initiations through small-molecule diffusion are gaining momentum. Here, selected examples of XFEL and synchrotron time-resolved crystallography studies will be used to highlight the specificities of the various instruments and methods with respect to time resolution, and are compared with cryo-trapping studies.
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hal-04448576 , version 1 (09-02-2024)

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Nicolas Caramello, Antoine Royant. From femtoseconds to minutes: time-resolved macromolecular crystallography at XFELs and synchrotrons. Acta crystallographica Section D : Structural biology [1993-..], 2024, 80 (2), pp.60-79. ⟨10.1107/S2059798323011002⟩. ⟨hal-04448576⟩
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