ArticleStructural dynamics (Melville, N.Y.)2018
Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals.
Article in Structural dynamics (Melville, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Real-space imaging of the electron-pair density hole in molecular Auger-Meitner decay.Nature physics · 2026Article
- Calculation of effective pump dose in X-ray-pump/X-ray-probe experiments.Journal of synchrotron radiation · 2025Article
- A comparative review of time-resolved x-ray and electron scattering to probe structural dynamics.Structural dynamics (Melville, N.Y.) · 2024Review
- Revealing core-valence interactions in solution with femtosecond X-ray pump X-ray probe spectroscopy.Nature communications · 2023Article
- Site-specific interrogation of an ionic chiral fragment during photolysis using an X-ray free-electron laser.Communications chemistry · 2021Article
- Signatures of electronic and nuclear coherences in ultrafast molecular x-ray and electron diffraction.Structural dynamics (Melville, N.Y.) · 2021Article
- Structural dynamics in proteins induced by and probed with X-ray free-electron laser pulses.Nature communications · 2020Article
- X-rays put molecules into a spin.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Femtosecond phase-transition in hard x-ray excited bismuth.Scientific reports · 2019Article
- Perspective: Towards single shot time-resolved microscopy using short wavelength table-top light sources.Structural dynamics (Melville, N.Y.) · 2019Article
Corrections and comments
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Authors and funding
20 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The development of X-ray free-electron lasers (XFELs) has opened the possibility to investigate the ultrafast dynamics of biomacromolecules using X-ray diffraction. Whereas an increasing number of structures solved by means of serial femtosecond crystallography at XFELs is available, the effect of radiation damage on protein crystals during ultrafast exposures has remained an open question. We used a split-and-delay line based on diffractive X-ray optics at the Linac Coherent Light Source XFEL to investigate the time dependence of X-ray radiation damage to lysozyme crystals. For these tests, crystals were delivered to the X-ray beam using a fixed-target approach. The presented experiments provide probe signals at eight different delay times between 19 and 213 femtoseconds after a single pump event, thereby covering the time-scales relevant for femtosecond serial crystallography. Even though significant impact on the crystals was observed at long time scales after exposure with a single X-ray pulse, the collected diffraction data did not show significant signal reduction that could be assigned to beam damage on the crystals in the sampled time window and resolution range. This observation is in agreement with estimations of the applied radiation dose, which in our experiment was clearly below the values expected to cause damage on the femtosecond time scale. The experiments presented here demonstrate the feasibility of time-resolved pump-multiprobe X-ray diffraction experiments on protein crystals.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.