The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.
Gisriel, Chris, et al. "Membrane protein megahertz crystallography at the European XFEL." Nature Communications, vol. 10, no. 1, Nov. 2019. https://doi.org/10.1038/s41467-019-12955-3
Gisriel, Chris, Coe, Jesse, Letrun, Romain, et al., "Membrane protein megahertz crystallography at the European XFEL," Nature Communications 10, no. 1 (2019), https://doi.org/10.1038/s41467-019-12955-3
@article{osti_1596363,
author = {Gisriel, Chris and Coe, Jesse and Letrun, Romain and Yefanov, Oleksandr M. and Luna-Chavez, Cesar and Stander, Natasha E. and Lisova, Stella and Mariani, Valerio and Kuhn, Manuela and Aplin, Steve and others},
title = {Membrane protein megahertz crystallography at the European XFEL},
annote = {The world’s first superconducting megahertz repetition rate hard X-ray free-electron laser (XFEL), the European XFEL, began operation in 2017, featuring a unique pulse train structure with 886 ns between pulses. With its rapid pulse rate, the European XFEL may alleviate some of the increasing demand for XFEL beamtime, particularly for membrane protein serial femtosecond crystallography (SFX), leveraging orders-of-magnitude faster data collection. Here, we report the first membrane protein megahertz SFX experiment, where we determined a 2.9 Å-resolution SFX structure of the large membrane protein complex, Photosystem I, a > 1 MDa complex containing 36 protein subunits and 381 cofactors. We address challenges to megahertz SFX for membrane protein complexes, including growth of large quantities of crystals and the large molecular and unit cell size that influence data collection and analysis. The results imply that megahertz crystallography could have an important impact on structure determination of large protein complexes with XFELs.},
doi = {10.1038/s41467-019-12955-3},
url = {https://www.osti.gov/biblio/1596363},
journal = {Nature Communications},
issn = {ISSN 2041-1723},
number = {1},
volume = {10},
place = {United States},
publisher = {Nature Publishing Group},
year = {2019},
month = {11}}
Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States); SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States); Univ. of Wisconsin, Milwaukee, WI (United States)
Sponsoring Organization:
Australian Research Council (ARC); Deutsche Forschungsgemeinschaft (DFG); European Research Council (ERC); German Federal Ministry of Education and Research (BMBF); National Institutes of Health (NIH); USDOE National Nuclear Security Administration (NNSA); USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, Vol. 633https://doi.org/10.1016/j.nima.2010.06.107
Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment, Vol. 942https://doi.org/10.1016/j.nima.2019.06.065
Coherent X-ray Imaging Data Bank (Lawrence Berkeley National Laboratory); CFEL, European XFEL, DESY, Uppsala University, Heidelberg Universityhttps://doi.org/10.11577/1721364