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Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements

MPS-Authors

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

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

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

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Epp,  Sascha
Division Prof. Dr. Thomas Pfeifer, MPI for Nuclear Physics, Max Planck Society;

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

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

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

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

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

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

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

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

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Citation

Barty, A., Caleman, C., Aquila, A., Timneanu, N., Lomb, L., White, T. A., et al. (2012). Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements. Nature Photonics, 6(1), 35-40. doi:10.1038/nphoton.2011.297.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-F225-8
Abstract
X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis1. For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information1-4. Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural information to be collected from crystalline samples using high radiation doses without the requirement for the pulse to terminate before the onset of sample damage. Instead, the diffracted X-rays are gated by a rapid loss of crystalline periodicity, producing apparent pulse lengths significantly shorter than the duration of the incident pulse. The shortest apparent pulse lengths occur at the highest resolution, and our measurements indicate that current X-ray free-electron laser technology5 should enable structural determination from submicrometre protein crystals with atomic resolution.