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Träfflista för sökning "WFRF:(Ekström J.Carl) "

Search: WFRF:(Ekström J.Carl)

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1.
  • Enquist, Henrik, et al. (author)
  • FemtoMAX - An X-ray beamline for structural dynamics at the short-pulse facility of MAX IV
  • 2018
  • In: Journal of Synchrotron Radiation. - 0909-0495. ; 25:2, s. 570-579
  • Journal article (peer-reviewed)abstract
    • The FemtoMAX beamline facilitates studies of the structural dynamics of materials. Such studies are of fundamental importance for key scientific problems related to programming materials using light, enabling new storage media and new manufacturing techniques, obtaining sustainable energy by mimicking photosynthesis, and gleaning insights into chemical and biological functional dynamics. The FemtoMAX beamline utilizes the MAX IV linear accelerator as an electron source. The photon bursts have a pulse length of 100fs, which is on the timescale of molecular vibrations, and have wavelengths matching interatomic distances (Å). The uniqueness of the beamline has called for special beamline components. This paper presents the beamline design including ultrasensitive X-ray beam-position monitors based on thin Ce:YAG screens, efficient harmonic separators and novel timing tools.The FemtoMAX beamline facilitates studies of the structural dynamics of materials on the femtosecond timescale. The first commissioning results are presented.
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2.
  • Jensen, Maja, 1978, et al. (author)
  • High-resolution macromolecular crystallography at the FemtoMAX beamline with time-over-threshold photon detection
  • 2021
  • In: Journal of Synchrotron Radiation. - 1600-5775 .- 0909-0495. ; 28, s. 64-70
  • Journal article (peer-reviewed)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 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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