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Showing 1–10 of 10 results
Advanced filters: Author: G. Weidenspointner Clear advanced filters

  • Researchers describe a mechanism capable of compressing fast and intense X-ray pulses through the rapid loss of crystalline periodicity. It is hoped that this concept, combined with X-ray free-electron laser technology, will allow scientists to obtain structural information at atomic resolutions.

    • Anton Barty
    • Carl Caleman
    • Henry N. Chapman
    Research
    Nature Photonics
    Volume: 6, P: 35-40

  • Lipidic sponge phase crystallization yields membrane protein microcrystals that can be injected into an X-ray free electron laser beam, yielding diffraction patterns that can be processed to recover the crystal structure.

    • Linda C Johansson
    • David Arnlund
    • Richard Neutze
    Research
    Nature Methods
    Volume: 9, P: 263-265

  • Free-electron lasers enable diffractive imaging of single nanostructures, but algorithms, such as correlation analyses, are needed to determine their diffraction volume from accumulated data. Starodub et al.present such a method for X-ray diffractive imaging of nanometre-scale polystyrene dimers.

    • D. Starodub
    • A. Aquila
    • M.J. Bogan
    Research
    Nature Communications
    Volume: 3, P: 1-7

  • The start-up of the new femtosecond hard X-ray laser facility in Stanford, the Linac Coherent Light Source, has brought high expectations for a new era for biological imaging. The intense, ultrashort X-ray pulses allow diffraction imaging of small structures before radiation damage occurs. This new capability is tested for the problem of imaging a non-crystalline biological sample. Images of mimivirus are obtained, the largest known virus with a total diameter of about 0.75 micrometres, by injecting a beam of cooled mimivirus particles into the X-ray beam. The measurements indicate no damage during imaging and prove the concept of this imaging technique.

    • M. Marvin Seibert
    • Tomas Ekeberg
    • Janos Hajdu
    Research
    Nature
    Volume: 470, P: 78-81

  • The start-up of the new femtosecond hard X-ray laser facility in Stanford, the Linac Coherent Light Source, has brought high expectations for a new era for biological imaging. The intense, ultrashort X-ray pulses allow diffraction imaging of small structures before radiation damage occurs. This new capability is tested for the problem of structure determination from nanocrystals of macromolecules that cannot be grown in large crystals. Over three million diffraction patterns were collected from a stream of nanocrystals of the membrane protein complex photosystem I, which allowed the assembly of a three-dimensional data set for this protein, and proves the concept of this imaging technique.

    • Henry N. Chapman
    • Petra Fromme
    • John C. H. Spence
    Research
    Nature
    Volume: 470, P: 73-77