Radiation damage in serial femtosecond crystallography studied in hemoglobin.
) and fixed photon energy (7.15 keV). Structural refinement produced very similar models and resolution-dependent data-quality indicators remained comparable. Both datasets also retained sufficient anomalous signal for phasing. These observations support the conclusion that high-resolution scattering was preserved under both pulse durations. Hybrid collisional-radiative and molecular-dynamics simulations show that under typical experimental conditions, atomic form-factor changes are negligible (<1%) and atomic displacements fall below the resolution limit imposed by the X-ray photon energy and the geometry of the detector. The combined experimental and theoretical results indicate that 10 fs pulses are adequate to obtain damage-free protein structures using femtosecond crystallography under the intensity conditions explored.
Authors
- Sebastian Cardoch (ORCID: https://orcid.org/0000-0003-0707-1832)
- J. Knoška (ORCID: https://orcid.org/0000-0001-7258-6256)
- Nicuşor Tı̂mneanu (ORCID: https://orcid.org/0000-0001-7328-0400)
- Marina Galchenkova (ORCID: https://orcid.org/0000-0001-5488-0160)
- Markus Metz (ORCID: https://orcid.org/0000-0002-4038-8754)
- Carl Caleman (ORCID: https://orcid.org/0000-0003-2638-1940)
- Emiliano De Santis (ORCID: https://orcid.org/0000-0001-5029-7429)
- Iosifina Sarrou (ORCID: https://orcid.org/0000-0002-6963-5341)
- Henry Chapman
- Gisel Pena
- Oleksandr Yefanov
- Spencer Passmore
- Dominik Oberthür
- Janina Sprenger
- Ibrahim Dawod
- Salah Awel
- Oscar Grånäs
- Max Wiedorn
Institutions
- University of Rome Tor Vergata (IT)
- Uppsala University (SE)
- Universität Hamburg (DE)
- Deutsches Elektronen-Synchrotron DESY (DE)
- Center for Free-Electron Laser Science (DE)
- Hamburg Centre for Ultrafast Imaging
- Swinburne University of Technology (AU)
- European X-Ray Free-Electron Laser (DE)
Publication Details
- Journal
- PubMed
- Published
- 2026-10-01
- DOI
- https://doi.org/10.1107/s2059798326008569
- Primary Topic
- Enzyme Structure and Function
- Type
- article
- Field-Weighted Citation Impact
- 0.00