Journal
SCIENTIFIC REPORTS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/srep44628
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Funding
- US Department of Energy (DOE) [DE-AC02-76SF00515]
- Helmholtz Association
- Virtual Institute
- Deutsche Forschungsgemeinschaft (DFG)DFG-EXC1074 [DFG-EXC1074, SFB740, SFB1078, D3/E3-1]
- DFG [SFB740, SFB1078]
- European Research Council under European Union [609920, 317079]
- European Union [637295]
- BMBF [05E13GU1, 05K13GUK, 05K2012]
- International Max Planck Research School UFAST
- BioXFEL Science Technology Center (National Science Foundation) [1231306]
- Slovenian Grant Agency (ARRS) [P2-0379, J2-7384]
- SLAC
- Stanford Institute for Chemical Biology
- NIH [R35GM118030, P41GM103393, R01 AI21144, GM49985, S10RR028096]
- Human Frontier Science Program [LT00160]
- Marie Curie Actions (MSCA) [637295] Funding Source: Marie Curie Actions (MSCA)
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Serial femtosecond crystallography requires reliable and efficient delivery of fresh crystals across the beam of an X-ray free-electron laser over the course of an experiment. We introduce a doubleflow focusing nozzle to meet this challenge, with significantly reduced sample consumption, while improving jet stability over previous generations of nozzles. We demonstrate its use to determine the first room-temperature structure of RNA polymerase II at high resolution, revealing new structural details. Moreover, the double-flow focusing nozzles were successfully tested with three other protein samples and the first room temperature structure of an extradiol ring-cleaving dioxygenase was solved by utilizing the improved operation and characteristics of these devices.
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