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    Femtosecond X-ray diffraction from an aerosolized beam of protein nanocrystals

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    Author
    Awel, S; Kirian, RA; Wiedorn, MO; Beyerlein, KR; Roth, N; Horke, DA; Oberthuer, D; Knoska, J; Mariani, V; Morgan, A; ...
    Date
    2018-02-01
    Source Title
    Journal of Applied Crystallography
    Publisher
    INT UNION CRYSTALLOGRAPHY
    University of Melbourne Author/s
    Morgan, Andrew
    Affiliation
    School of Physics
    Metadata
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    Document Type
    Journal Article
    Citations
    Awel, S., Kirian, R. A., Wiedorn, M. O., Beyerlein, K. R., Roth, N., Horke, D. A., Oberthuer, D., Knoska, J., Mariani, V., Morgan, A., Adriano, L., Tolstikova, A., Xavier, P. L., Yefanov, O., Aquila, A., Barty, A., Roy-Chowdhury, S., Hunter, M. S., James, D. ,... Chapman, H. N. (2018). Femtosecond X-ray diffraction from an aerosolized beam of protein nanocrystals. JOURNAL OF APPLIED CRYSTALLOGRAPHY, 51 (Pt 1), pp.133-139. https://doi.org/10.1107/S1600576717018131.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/254983
    DOI
    10.1107/S1600576717018131
    Abstract
    High-resolution Bragg diffraction from aerosolized single granulovirus nanocrystals using an X-ray free-electron laser is demonstrated. The outer dimensions of the in-vacuum aerosol injector components are identical to conventional liquid-microjet nozzles used in serial diffraction experiments, which allows the injector to be utilized with standard mountings. As compared with liquid-jet injection, the X-ray scattering background is reduced by several orders of magnitude by the use of helium carrier gas rather than liquid. Such reduction is required for diffraction measurements of small macromolecular nanocrystals and single particles. High particle speeds are achieved, making the approach suitable for use at upcoming high-repetition-rate facilities.

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