Native phasing of x-ray free-electron laser data for a G protein–coupled receptor
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 A2Aadenosine receptor at 1.9 Å resolution. The advancement was made possible by recent improvements in SFX data analysis and the design of injectors and delivery media for streaming hydrated microcrystals. This general method should accelerate structural studies of novel difficult-to-crystallize macromolecules and their complexes.
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- Univ. of Zurich (Switzerland)
- Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
- Univ. of Southern California, Los Angeles, CA (United States)
- Moscow Inst. of Physics and Technology (MIPT), Dolgoprudny (Russian Federation); Univ. of Southern California, Los Angeles, CA (United States)
- SLAC National Accelerator Lab., Menlo Park, CA (United States)
- Chinese Academy of Sciences (CAS), Beijing (China)
- ShanghaiTech Univ., Shanghai (China); Chinese Academy of Sciences (CAS), Beijing (China)
- Arizona State Univ., Tempe, AZ (United States)
- Univ. of Southern California, Los Angeles, CA (United States); Shanghai Tech. Univ. (China)
- Publication Date:
- Research Org.:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES); National Institutes of Health (NIH); Ministry of Science and Technology of China; National Science Foundation (NSF), Science and Technology Center; PIER Helmholtz Graduate School; Helmholtz Association; Russian Ministry of Education and Science
- OSTI Identifier:
- 1625958
- Grant/Contract Number:
- AC02-76SF00515; R01 GM108635; U54 GM094618; U54 GM094599; R01 GM095583; 2014CB910400; 1231306; 5-100; P41 GM103393
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Science Advances
- Additional Journal Information:
- Journal Volume: 2; Journal Issue: 9; Journal ID: ISSN 2375-2548
- Publisher:
- AAAS
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 47 OTHER INSTRUMENTATION; Science & Technology - Other Topics
Citation Formats
Batyuk, Alexander, Galli, Lorenzo, Ishchenko, Andrii, Han, Gye Won, Gati, Cornelius, Popov, Petr A., Lee, Ming-Yue, Stauch, Benjamin, White, Thomas A., Barty, Anton, Aquila, Andrew, Hunter, Mark S., Liang, Mengning, Boutet, Sébastien, Pu, Mengchen, Liu, Zhi-jie, Nelson, Garrett, James, Daniel, Li, Chufeng, Zhao, Yun, Spence, John C. H., Liu, Wei, Fromme, Petra, Katritch, Vsevolod, Weierstall, Uwe, Stevens, Raymond C., and Cherezov, Vadim. Native phasing of x-ray free-electron laser data for a G protein–coupled receptor. United States: N. p., 2016.
Web. doi:10.1126/sciadv.1600292.
Batyuk, Alexander, Galli, Lorenzo, Ishchenko, Andrii, Han, Gye Won, Gati, Cornelius, Popov, Petr A., Lee, Ming-Yue, Stauch, Benjamin, White, Thomas A., Barty, Anton, Aquila, Andrew, Hunter, Mark S., Liang, Mengning, Boutet, Sébastien, Pu, Mengchen, Liu, Zhi-jie, Nelson, Garrett, James, Daniel, Li, Chufeng, Zhao, Yun, Spence, John C. H., Liu, Wei, Fromme, Petra, Katritch, Vsevolod, Weierstall, Uwe, Stevens, Raymond C., & Cherezov, Vadim. Native phasing of x-ray free-electron laser data for a G protein–coupled receptor. United States. https://doi.org/10.1126/sciadv.1600292
Batyuk, Alexander, Galli, Lorenzo, Ishchenko, Andrii, Han, Gye Won, Gati, Cornelius, Popov, Petr A., Lee, Ming-Yue, Stauch, Benjamin, White, Thomas A., Barty, Anton, Aquila, Andrew, Hunter, Mark S., Liang, Mengning, Boutet, Sébastien, Pu, Mengchen, Liu, Zhi-jie, Nelson, Garrett, James, Daniel, Li, Chufeng, Zhao, Yun, Spence, John C. H., Liu, Wei, Fromme, Petra, Katritch, Vsevolod, Weierstall, Uwe, Stevens, Raymond C., and Cherezov, Vadim. Fri .
"Native phasing of x-ray free-electron laser data for a G protein–coupled receptor". United States. https://doi.org/10.1126/sciadv.1600292. https://www.osti.gov/servlets/purl/1625958.
@article{osti_1625958,
title = {Native phasing of x-ray free-electron laser data for a G protein–coupled receptor},
author = {Batyuk, Alexander and Galli, Lorenzo and Ishchenko, Andrii and Han, Gye Won and Gati, Cornelius and Popov, Petr A. and Lee, Ming-Yue and Stauch, Benjamin and White, Thomas A. and Barty, Anton and Aquila, Andrew and Hunter, Mark S. and Liang, Mengning and Boutet, Sébastien and Pu, Mengchen and Liu, Zhi-jie and Nelson, Garrett and James, Daniel and Li, Chufeng and Zhao, Yun and Spence, John C. H. and Liu, Wei and Fromme, Petra and Katritch, Vsevolod and Weierstall, Uwe and Stevens, Raymond C. and Cherezov, Vadim},
abstractNote = {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 A2Aadenosine receptor at 1.9 Å resolution. The advancement was made possible by recent improvements in SFX data analysis and the design of injectors and delivery media for streaming hydrated microcrystals. This general method should accelerate structural studies of novel difficult-to-crystallize macromolecules and their complexes.},
doi = {10.1126/sciadv.1600292},
journal = {Science Advances},
number = 9,
volume = 2,
place = {United States},
year = {Fri Sep 23 00:00:00 EDT 2016},
month = {Fri Sep 23 00:00:00 EDT 2016}
}
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