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    A step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum

    Access Status
    Open access via publisher
    Authors
    Panjikar, S.
    Thomsen, L.
    O'Donnell, Kane
    Riboldi-Tunnicliffe, A.
    Date
    2015
    Type
    Journal Article
    
    Metadata
    Show full item record
    Citation
    Panjikar, S. and Thomsen, L. and O'Donnell, K. and Riboldi-Tunnicliffe, A. 2015. A step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum. Journal of Applied Crystallography. 48: pp. 913-916.
    Source Title
    Journal of Applied Crystallography
    DOI
    10.1107/S1600576715006147
    ISSN
    0021-8898
    School
    Department of Physics and Astronomy
    URI
    http://hdl.handle.net/20.500.11937/34173
    Collection
    • Curtin Research Publications
    Abstract

    Using the UHV experimental endstation on the soft X-ray beamline at the Australian Synchrotron, lysozyme and proteinase K crystals have been exposed to a vacuum of 10-5 mbar, prior to flash-cooling in a bath of liquid nitrogen. Subsequent data collection on the MX2 beamline at the Australian Synchrotron demonstrated that, for lysozyme and proteinase K, it is possible to subject these mounted crystals to a vacuum pressure of 10-5 mbar without destroying the crystal lattice. Despite the lower data quality of the vacuum-pumped crystals compared with control crystals, it is demonstrated that the protein crystals can survive in a vacuum under suitable conditions.

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