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Batyuk A, Galli L, Ishchenko A, et al. Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Sci Adv. 2016;2(9):e1600292doi: 10.1126/sciadv.1600292.
Batyuk, A., Galli, L., Ishchenko, A., Han, G. W., Gati, C., Popov, P. A., Lee, M. Y., Stauch, B., White, T. A., Barty, A., Aquila, A., Hunter, M. S., Liang, M., Boutet, S., Pu, M., Liu, Z. J., Nelson, G., James, D., Li, C., Zhao, Y., Spence, J. C., Liu, W., Fromme, P., Katritch, V., Weierstall, U., Stevens, R. C., & Cherezov, V. (2016). Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Science advances, 2(9), e1600292. https://doi.org/10.1126/sciadv.1600292
Batyuk, Alexander, et al. "Native phasing of x-ray free-electron laser data for a G protein-coupled receptor." Science advances vol. 2,9 (2016): e1600292. doi: https://doi.org/10.1126/sciadv.1600292
Batyuk A, Galli L, Ishchenko A, Han GW, Gati C, Popov PA, Lee MY, Stauch B, White TA, Barty A, Aquila A, Hunter MS, Liang M, Boutet S, Pu M, Liu ZJ, Nelson G, James D, Li C, Zhao Y, Spence JC, Liu W, Fromme P, Katritch V, Weierstall U, Stevens RC, Cherezov V. Native phasing of x-ray free-electron laser data for a G protein-coupled receptor. Sci Adv. 2016 Sep 23;2(9):e1600292. doi: 10.1126/sciadv.1600292. eCollection 2016 Sep. PMID: 27679816; PMCID: PMC5035125.
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Sci Adv. 2016 Sep 23;2(9):e1600292. doi: 10.1126/sciadv.1600292. eCollection 2016 Sep.

Native phasing of x-ray free-electron laser data for a G protein-coupled receptor.

Science advances

Alexander Batyuk, Lorenzo Galli, Andrii Ishchenko, Gye Won Han, Cornelius Gati, Petr A Popov, Ming-Yue Lee, Benjamin Stauch, Thomas A White, Anton Barty, Andrew Aquila, Mark S Hunter, Mengning Liang, Sébastien Boutet, Mengchen Pu, Zhi-Jie Liu, Garrett Nelson, Daniel James, Chufeng Li, Yun Zhao, John C H Spence, Wei Liu, Petra Fromme, Vsevolod Katritch, Uwe Weierstall, Raymond C Stevens, Vadim Cherezov

Affiliations

  1. Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, 8057 Zürich, Switzerland.
  2. Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Notkestrasse 85, 22607 Hamburg, Germany.
  3. Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.; Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.
  4. Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.; Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.
  5. Linac Coherent Light Source, SLAC National Accelerator Laboratory, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
  6. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.
  7. National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.; iHuman Institute, ShanghaiTech University, Shanghai 201210, China.
  8. Department of Physics, Arizona State University, Tempe, AZ 85287, USA.
  9. Center for Applied Structural Discovery at the Biodesign Institute, School of Molecular Sciences, Arizona State University, 727 East Tyler Street, Tempe, AZ 85287, USA.
  10. Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.; Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.; Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.
  11. Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.; Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.; Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.; iHuman Institute, ShanghaiTech University, Shanghai 201210, China.
  12. Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.; Bridge Institute, University of Southern California, Los Angeles, CA 90089, USA.; Moscow Institute of Physics and Technology, Dolgoprudny 141700, Russia.; Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, USA.; Department of Physics and Astronomy, University of Southern California, Los Angeles, CA 90089, USA.

PMID: 27679816 PMCID: PMC5035125 DOI: 10.1126/sciadv.1600292

Abstract

Serial femtosecond crystallography (SFX) takes advantage of extremely bright and ultrashort pulses produced by x-ray free-electron lasers (XFELs), allowing for the collection of high-resolution diffraction intensities from micrometer-sized crystals at room temperature with minimal radiation damage, using the principle of "diffraction-before-destruction." However, de novo structure factor phase determination using XFELs has been difficult so far. We demonstrate the ability to solve the crystallographic phase problem for SFX data collected with an XFEL using the anomalous signal from native sulfur atoms, leading to a bias-free room temperature structure of the human A

Keywords: Crystallography; GPCR; SAD; de novo structure; lipidic cubic phase; native phasing; protein; serial femtosecond crystallography; sulfur; x-ray free electron laser

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