Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals
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 splitand-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 damagemore »
- Authors:
-
- Paul Scherrer Inst. (Switzerland); Univ. of Basel (Switzerland); Swiss Nanoscience Inst., Basel, (Switzerland)
- Paul Scherrer Inst. (Switzerland); Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
- Paul Scherrer Inst. (Switzerland); European XFEL GmbH, Schenefeld (Germany)
- Univ. of Basel (Switzerland)
- Paul Scherrer Inst. (Switzerland)
- Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
- SLAC National Accelerator Lab., Menlo Park, CA (United States). Linac Coherent Light Source (LCLS)
- Univ. of Basel (Switzerland); Swiss Nanoscience Inst., Basel, (Switzerland)
- Publication Date:
- Research Org.:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States). Linac Coherent Light Source (LCLS); Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); European Community’s Seventh Framework Programme; Swiss Nanoscience Institute
- OSTI Identifier:
- 1625000
- Alternate Identifier(s):
- OSTI ID: 1475093
- Grant/Contract Number:
- AC02-76SF00515; AC52-07NA27344; 290605
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Structural Dynamics
- Additional Journal Information:
- Journal Volume: 5; Journal Issue: 5; Journal ID: ISSN 2329-7778
- Publisher:
- American Crystallographic Association/AIP
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 43 PARTICLE ACCELERATORS; 59 BASIC BIOLOGICAL SCIENCES; Chemistry; Physics; Ultrafast time-resolved crystallography; Free electron lasers; Physical radiation effects; Delay lines; Protein crystallography; X-ray optics; Pump probe experiments; Radiation damage; X-ray diffraction; Ultrafast optics
Citation Formats
Opara, Nadia L., Mohacsi, Istvan, Makita, Mikako, Castano-Diez, Daniel, Diaz, Ana, Juranić, Pavle, Marsh, May, Meents, Alke, Milne, Christopher J., Mozzanica, Aldo, Padeste, Celestino, Panneels, Valérie, Sikorski, Marcin, Song, Sanghoon, Stahlberg, Henning, Vartiainen, Ismo, Vera, Laura, Wang, Meitian, Willmott, Philip R., and David, Christian. Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals. United States: N. p., 2018.
Web. doi:10.1063/1.5050618.
Opara, Nadia L., Mohacsi, Istvan, Makita, Mikako, Castano-Diez, Daniel, Diaz, Ana, Juranić, Pavle, Marsh, May, Meents, Alke, Milne, Christopher J., Mozzanica, Aldo, Padeste, Celestino, Panneels, Valérie, Sikorski, Marcin, Song, Sanghoon, Stahlberg, Henning, Vartiainen, Ismo, Vera, Laura, Wang, Meitian, Willmott, Philip R., & David, Christian. Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals. United States. https://doi.org/10.1063/1.5050618
Opara, Nadia L., Mohacsi, Istvan, Makita, Mikako, Castano-Diez, Daniel, Diaz, Ana, Juranić, Pavle, Marsh, May, Meents, Alke, Milne, Christopher J., Mozzanica, Aldo, Padeste, Celestino, Panneels, Valérie, Sikorski, Marcin, Song, Sanghoon, Stahlberg, Henning, Vartiainen, Ismo, Vera, Laura, Wang, Meitian, Willmott, Philip R., and David, Christian. Mon .
"Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals". United States. https://doi.org/10.1063/1.5050618. https://www.osti.gov/servlets/purl/1625000.
@article{osti_1625000,
title = {Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals},
author = {Opara, Nadia L. and Mohacsi, Istvan and Makita, Mikako and Castano-Diez, Daniel and Diaz, Ana and Juranić, Pavle and Marsh, May and Meents, Alke and Milne, Christopher J. and Mozzanica, Aldo and Padeste, Celestino and Panneels, Valérie and Sikorski, Marcin and Song, Sanghoon and Stahlberg, Henning and Vartiainen, Ismo and Vera, Laura and Wang, Meitian and Willmott, Philip R. and David, Christian},
abstractNote = {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 splitand-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.},
doi = {10.1063/1.5050618},
journal = {Structural Dynamics},
number = 5,
volume = 5,
place = {United States},
year = {Mon Oct 01 00:00:00 EDT 2018},
month = {Mon Oct 01 00:00:00 EDT 2018}
}
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Cited by: 9 works
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Figures / Tables:
FIG. 1: Scheme of the X-ray optics set-up (adapted from Ref. 34), showing the data collection in transmission geometry for protein crystal diffraction. The detector was placed off-axis at an angle of 13° at a 122 cm distance from the sample. (a) Top view, (b) perspective view, pumping beam onmore »
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Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein
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Works referencing / citing this record:
Perspective: Towards single shot time-resolved microscopy using short wavelength table-top light sources
text, January 2019
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- GSI Helmholtzzentrum fuer Schwerionenforschung, GSI, Darmstadt
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X-rays put molecules into a spin
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Perspective: Towards single shot time-resolved microscopy using short wavelength table-top light sources
text, January 2019
- Helk, T.; Zürch, M.; Spielmann, C.
- GSI Helmholtzzentrum fuer Schwerionenforschung, GSI, Darmstadt
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