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Updated: May 25, 2026
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Measurements of Long-range Electronic Correlations During Femtosecond Diffraction Experiments Performed on Nanocrystals of Buckminsterfullerene
Published on: August 22, 2017
Time-resolved protein nanocrystallography using an X-ray free-electron laser
Andrew Aquila1, Mark S Hunter, R Bruce Doak
1Center for Free-Electron Laser Science, DESY, Notkestraße 85, 22607 Hamburg, Germany. Andrew.Aquila@desy.de
Optics Express
|February 15, 2012
Summary
We captured X-ray diffraction snapshots of photoactivated Photosystem I-Ferredoxin nanocrystals using an X-ray free electron laser. This reveals microsecond structural changes linked to electron transfer and crystal disintegration.
Area of Science:
- Structural Biology
- Biophysics
- Photochemistry
Background:
- Large membrane protein complexes are crucial for biological processes.
- Understanding their dynamics requires advanced structural techniques.
- Photosystem I-Ferredoxin is key in photosynthetic electron transport.
Purpose of the Study:
- To apply time-resolved serial X-ray crystallography to study photoactivated membrane protein dynamics.
- To capture structural snapshots of Photosystem I-Ferredoxin nanocrystals after light excitation.
- To correlate structural changes with electron transfer kinetics.
Main Methods:
- Utilizing an X-ray free electron laser synchronized with an optical pump laser.
- Employing femtosecond serial X-ray crystallography on nanocrystals in a liquid jet.
- Observing light-induced structural changes at microsecond time delays.
Main Results:
- X-ray diffraction snapshots revealed structural changes in Photosystem I-Ferredoxin nanocrystals 5-10 µs post-excitation.
- Observed changes correlate with microsecond electron transfer kinetics.
- Undocking and subsequent crystal rearrangements leading to disintegration were documented.
Conclusions:
- Femtosecond serial X-ray crystallography can resolve dynamics of irreversible photochemical reactions.
- This technique provides insights into reaction dynamics in biological systems.
- The study offers a new approach for time-resolved structural biology.
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