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High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection

Jensen, Maja LU ; Ahlberg Gagnér, Viktor ; Cabello Sánchez, Juan ; Bengtsson, Åsa U.J. LU ; Ekström, J. Carl ; Björg Úlfarsdóttir, Tinna ; Garcia-Bonete, Maria-Jose ; Jurgilaitis, Andrius LU ; Kroon, David LU and Pham, Van-Thai LU , et al. (2021) In Journal of Synchrotron Radiation 28. p.64-70
Abstract

Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation... (More)

Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative intensity distribution compared with theoretical distribution, I/σ, Rmerge/Rmeas and CC1/2 statistics versus resolution. The FemtoMAX beamline provides an interesting alternative to X-ray free-electron lasers when studying reversible processes in protein crystals.

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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
femtosecond, macromolecular crystallography, multilayer monochromator, time-over-threshold
in
Journal of Synchrotron Radiation
volume
28
pages
7 pages
publisher
International Union of Crystallography
external identifiers
  • scopus:85099428554
  • pmid:33399553
ISSN
1600-5775
DOI
10.1107/S1600577520014599
language
English
LU publication?
yes
id
043b859e-d304-45d8-a565-b437ffb1b923
alternative location
https://scripts.iucr.org/cgi-bin/paper?S1600577520014599
date added to LUP
2021-01-31 08:27:06
date last changed
2024-03-21 01:50:55
@article{043b859e-d304-45d8-a565-b437ffb1b923,
  abstract     = {{<p>Protein dynamics contribute to protein function on different time scales. Ultrafast X-ray diffraction snapshots can visualize the location and amplitude of atom displacements after perturbation. Since amplitudes of ultrafast motions are small, high-quality X-ray diffraction data is necessary for detection. Diffraction from bovine trypsin crystals using single femtosecond X-ray pulses was recorded at FemtoMAX, which is a versatile beamline of the MAX IV synchrotron. The time-over-threshold detection made it possible that single photons are distinguishable even under short-pulse low-repetition-rate conditions. The diffraction data quality from FemtoMAX beamline enables atomic resolution investigation of protein structures. This evaluation is based on the shape of the Wilson plot, cumulative intensity distribution compared with theoretical distribution, <i>I</i>/<i>σ</i>, <i>R<sub>merge</sub></i>/<i>R<sub>meas</sub></i> and CC<sub>1/2</sub> statistics versus resolution. The FemtoMAX beamline provides an interesting alternative to X-ray free-electron lasers when studying reversible processes in protein crystals.</p>}},
  author       = {{Jensen, Maja and Ahlberg Gagnér, Viktor and Cabello Sánchez, Juan and Bengtsson, Åsa U.J. and Ekström, J. Carl and Björg Úlfarsdóttir, Tinna and Garcia-Bonete, Maria-Jose and Jurgilaitis, Andrius and Kroon, David and Pham, Van-Thai and Checcia, Stefano and Coudert-Alteirac, Hélène and Schewa, Siawosch and Rössle, Manfred and Rodilla, Helena and Stake, Jan and Zhaunerchyk, Vitali and Larsson, Jörgen and Katona, Gergely}},
  issn         = {{1600-5775}},
  keywords     = {{femtosecond; macromolecular crystallography; multilayer monochromator; time-over-threshold}},
  language     = {{eng}},
  pages        = {{64--70}},
  publisher    = {{International Union of Crystallography}},
  series       = {{Journal of Synchrotron Radiation}},
  title        = {{High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection}},
  url          = {{http://dx.doi.org/10.1107/S1600577520014599}},
  doi          = {{10.1107/S1600577520014599}},
  volume       = {{28}},
  year         = {{2021}},
}