Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals
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 r...
| Main Authors: | , , , , , , , , , , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
AIP Publishing LLC and ACA
2018-09-01
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| Series: | Structural Dynamics |
| Online Access: | http://dx.doi.org/10.1063/1.5050618 |
| _version_ | 1818904858925727744 |
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| author | Nadia L. Opara Istvan Mohacsi Mikako Makita Daniel Castano-Diez Ana Diaz Pavle Juranić May Marsh Alke Meents Christopher J. Milne Aldo Mozzanica Celestino Padeste Valérie Panneels Marcin Sikorski Sanghoon Song Henning Stahlberg Ismo Vartiainen Laura Vera Meitian Wang Philip R. Willmott Christian David |
| author_facet | Nadia L. Opara Istvan Mohacsi Mikako Makita Daniel Castano-Diez Ana Diaz Pavle Juranić May Marsh Alke Meents Christopher J. Milne Aldo Mozzanica Celestino Padeste Valérie Panneels Marcin Sikorski Sanghoon Song Henning Stahlberg Ismo Vartiainen Laura Vera Meitian Wang Philip R. Willmott Christian David |
| author_sort | Nadia L. Opara |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-19T21:14:07Z |
| format | Article |
| id | doaj.art-037cf6dcdaae40e097c2329944107884 |
| institution | Directory Open Access Journal |
| issn | 2329-7778 |
| language | English |
| last_indexed | 2024-12-19T21:14:07Z |
| publishDate | 2018-09-01 |
| publisher | AIP Publishing LLC and ACA |
| record_format | Article |
| series | Structural Dynamics |
| spelling | doaj.art-037cf6dcdaae40e097c23299441078842022-12-21T20:05:24ZengAIP Publishing LLC and ACAStructural Dynamics2329-77782018-09-0155054303054303-1510.1063/1.5050618004805SDYDemonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystalsNadia L. Opara0Istvan Mohacsi1Mikako Makita2Daniel Castano-Diez3Ana Diaz4Pavle Juranić5May Marsh6Alke Meents7Christopher J. Milne8Aldo Mozzanica9Celestino Padeste10Valérie Panneels11Marcin Sikorski12Sanghoon Song13Henning Stahlberg14Ismo Vartiainen15Laura Vera16Meitian Wang17Philip R. Willmott18Christian David19 Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland C-CINA, Biozentrum, University of Basel, CH-4058 Basel, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Deutsches Elektronen-Synchrotron DESY, Notkestrasse 85, D-22607 Hamburg, Germany Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland LCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA LCLS, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, California 94025, USA C-CINA, Biozentrum, University of Basel, CH-4058 Basel, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, Switzerland Paul Scherrer Institut, CH-5232 Villigen-PSI, SwitzerlandThe 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.http://dx.doi.org/10.1063/1.5050618 |
| spellingShingle | Nadia L. Opara Istvan Mohacsi Mikako Makita Daniel Castano-Diez Ana Diaz Pavle Juranić May Marsh Alke Meents Christopher J. Milne Aldo Mozzanica Celestino Padeste Valérie Panneels Marcin Sikorski Sanghoon Song Henning Stahlberg Ismo Vartiainen Laura Vera Meitian Wang Philip R. Willmott Christian David Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals Structural Dynamics |
| title | Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals |
| title_full | Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals |
| title_fullStr | Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals |
| title_full_unstemmed | Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals |
| title_short | Demonstration of femtosecond X-ray pump X-ray probe diffraction on protein crystals |
| title_sort | demonstration of femtosecond x ray pump x ray probe diffraction on protein crystals |
| url | http://dx.doi.org/10.1063/1.5050618 |
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