Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12314
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Funding
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- European Community [290605, FP7-PEOPLE-2011-ITN 317079 NanoMem, SNF 31003A_141235, SNF 31003A_159558, SNF 310030_153145]
- NCCR MUST/ETH-FAST
- STC grant [NSF 1231306]
- Knut and Alice Wallenberg Foundation
- Swedish Strategic Research Foundation (SSF)
- Swedish Research Council (VR)
- PIER Helmholtz Graduate School
- Helmholtz Association
- X-ray Free-Electron Laser Priority Strategy Program
- Japan Science and Technology agency
- National Institutes of Health [P41GM103393]
- Grants-in-Aid for Scientific Research [15H01055, 15H03841, 15H05476] Funding Source: KAKEN
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Serial femtosecond crystallography (SFX) using X-ray free-electron laser sources is an emerging method with considerable potential for time-resolved pump-probe experiments. Here we present a lipidic cubic phase SFX structure of the light-driven proton pump bacteriorhodopsin (bR) to 2.3 angstrom resolution and a method to investigate protein dynamics with modest sample requirement. Time-resolved SFX (TR-SFX) with a pump-probe delay of 1ms yields difference Fourier maps compatible with the dark to M state transition of bR. Importantly, the method is very sample efficient and reduces sample consumption to about 1mg per collected time point. Accumulation of M intermediate within the crystal lattice is confirmed by time-resolved visible absorption spectroscopy. This study provides an important step towards characterizing the complete photocycle dynamics of retinal proteins and demonstrates the feasibility of a sample efficient viscous medium jet for TR-SFX.
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