Panjikar Santosh, Thomsen Lars, O'Donnell Kane Michael, Riboldi-Tunnicliffe Alan
Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia.
Australian Synchrotron, 800 Blackburn Road, Clayton, VIC 3168, Australia ; Department of Physics, Astronomy and Medical Radiation Physics, Curtin University, Bentley, WA 6102, Australia.
J Appl Crystallogr. 2015 May 9;48(Pt 3):913-916. doi: 10.1107/S1600576715006147. eCollection 2015 Jun 1.
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 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 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.
利用澳大利亚同步加速器软X射线束线上的超高真空实验终端站，在将溶菌酶和蛋白酶K晶体置于液氮浴中进行快速冷却之前，先将其暴露于10毫巴的真空中。随后在澳大利亚同步加速器的MX2束线上进行的数据收集表明，对于溶菌酶和蛋白酶K而言，有可能使这些安装好的晶体承受10毫巴的真空压力而不破坏晶格。尽管与对照晶体相比，经真空抽气的晶体数据质量较低，但结果表明蛋白质晶体在合适条件下能够在真空中存活。
