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

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.

SUBMITTER: Panjikar S

PROVIDER: S-EPMC4453978 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature

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

Panjikar Santosh S Thomsen Lars L O'Donnell Kane Michael KM Riboldi-Tunnicliffe Alan A

Journal of applied crystallography 20150509 Pt 3

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. ...[more]

PMID: 26089765

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