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Radiation damage in protein serial femtosecond crystallography using an x-ray free-electron laser

MPS-Authors
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Lomb,  Lukas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Barends,  Thomas
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kassemeyer,  Stephan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Erk,  Benjamin
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Foucar,  Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Rudek,  Benedikt
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Rolles,  Daniel
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Shoeman,  Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Doak,  R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Gebhardt,  Maike
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Kabsch,  Wolfgang
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Meinhart,  Anton
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Nass,  Karol
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Steinbrener,  Jan
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Schlichting,  Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Lomb, L., Barends, T., Kassemeyer, S., Aquila, A., Epp, S. W., Erk, B., et al. (2011). Radiation damage in protein serial femtosecond crystallography using an x-ray free-electron laser. Physical Review B, 84(21): e214111, pp. 1-6. doi:10.1103/PhysRevB.84.214111.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-1D94-B
Abstract
X−ray free−electron lasers deliver intense femtosecond pulses that promise to yield high resolution diffraction data of nanocrystals before the destruction of the sample by radiation damage. Diffraction intensities of lysozyme nanocrystals collected at the Linac Coherent Light Source using 2 keV photons were used for structure determination by molecular replacement and analyzed for radiation damage as a function of pulse length and fluence. Signatures of radiation damage are observed for pulses as short as 70 fs. Parametric scaling used in conventional crystallography does not account for the observed effects