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

Maja Jensen, Viktor Ahlberg Gagnér, Juan Cabello Sánchez, Åsa U.J. Bengtsson, J. Carl Ekström, Tinna Björg Úlfarsdóttir, Maria-Jose Garcia-Bonete, Andrius Jurgilaitis, David Kroon, Van-Thai Pham, Stefano Checcia, Hélène Coudert-Alteirac, Siawosch Schewa, Manfred Rössle, Helena Rodilla, Jan Stake, Vitali Zhaunerchyk, Jörgen Larsson, Gergely Katona

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)64-70
Number of pages7
JournalJournal of Synchrotron Radiation
Publication statusPublished - 2021

Subject classification (UKÄ)

  • Atom and Molecular Physics and Optics

Free keywords

  • femtosecond
  • macromolecular crystallography
  • multilayer monochromator
  • time-over-threshold


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