title: 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 10-5mbar, 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 10-5mbar 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.
authors.affiliation: Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia.
authors.forename: Santosh
authors.initials: S
authors.lastname: Panjikar
authors.affiliation: Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia.
authors.forename: Lars
authors.initials: L
authors.lastname: Thomsen
authors.affiliation: Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia ; Department of Physics, Astronomy and Medical Radiation Physics, Curtin University, Bentley, WA 6102, Australia.
authors.forename: Kane Michael
authors.initials: KM
authors.lastname: O'Donnell
authors.affiliation: Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia.
authors.forename: Alan
authors.initials: A
authors.lastname: Riboldi-Tunnicliffe
keywords: long-wavelength crystallography; lysozyme; proteinase K; sulfur single-wavelength anomalous diffraction; vacuum