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dc.contributor.authorPanjikar, S.
dc.contributor.authorThomsen, L.
dc.contributor.authorO'Donnell, Kane
dc.contributor.authorRiboldi-Tunnicliffe, A.
dc.date.accessioned2017-01-30T13:41:44Z
dc.date.available2017-01-30T13:41:44Z
dc.date.created2015-10-29T04:09:18Z
dc.date.issued2015
dc.identifier.citationPanjikar, 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.
dc.identifier.urihttp://hdl.handle.net/20.500.11937/34173
dc.identifier.doi10.1107/S1600576715006147
dc.description.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.

dc.publisherInternational Union of Crystallography
dc.titleA step towards long-wavelength protein crystallography: Subjecting protein crystals to a vacuum
dc.typeJournal Article
dcterms.source.volume48
dcterms.source.startPage913
dcterms.source.endPage916
dcterms.source.issn0021-8898
dcterms.source.titleJournal of Applied Crystallography
curtin.departmentDepartment of Physics and Astronomy
curtin.accessStatusOpen access via publisher


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