Radiation damage in serial femtosecond crystallography studied in hemoglobin.
Abstract
) 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.
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Authors: Marina Galchenkova, Ibrahim Dawod, Sebastian Cardoch, Janina Sprenger, Dominik Oberthür, Salah Awel, Emiliano De Santis, Oscar Grånäs, J. Knoška, Markus Metz, Spencer Passmore, Gisel Pena, Iosifina Sarrou, Max Wiedorn, Nicuşor Tı̂mneanu, Henry Chapman, Oleksandr Yefanov, Carl Caleman
Institutions: Swinburne University of Technology, Uppsala University, Universität Hamburg, University of Rome Tor Vergata, Deutsches Elektronen-Synchrotron DESY, Hamburg Centre for Ultrafast Imaging, European X-Ray Free-Electron Laser, Center for Free-Electron Laser Science