Serial femtosecond crystallography of G protein-coupled receptors

Wei Liu; Daniel Wacker; Cornelius Gati; Gye Won Han; Daniel James; Dingjie Wang; Garrett Nelson; Uwe Weierstall; Vsevolod Katritch; Anton Barty; Nadia Zatsepin; Dianfan Li; Marc Messerschmidt; Sébastien Boutet; Garth J. Williams; Jason E. Koglin; M. Marvin Seibert; Chong Wang; Syed T A Shah; Shibom Basu; Raimund Fromme; Christopher Kupitz; Kimberley N. Rendek; Ingo Grotjohann; Petra Fromme; Richard Kirian; Kenneth R. Beyerlein; Thomas A. White; Henry N. Chapman; Martin Caffrey; John Spence; Raymond C. Stevens; Vadim Cherezov

doi:10.1126/science.1244142

Serial femtosecond crystallography of G protein-coupled receptors

Wei Liu, Daniel Wacker, Cornelius Gati, Gye Won Han, Daniel James, Dingjie Wang, Garrett Nelson, Uwe Weierstall, Vsevolod Katritch, Anton Barty, Nadia Zatsepin, Dianfan Li, Marc Messerschmidt, Sébastien Boutet, Garth J. Williams, Jason E. Koglin, M. Marvin Seibert, Chong Wang, Syed T A Shah, Shibom BasuRaimund Fromme, Christopher Kupitz, Kimberley N. Rendek, Ingo Grotjohann, Petra Fromme, Richard Kirian, Kenneth R. Beyerlein, Thomas A. White, Henry N. Chapman, Martin Caffrey, John Spence, Raymond C. Stevens, Vadim Cherezov

Research output: Contribution to journal › Article › peer-review

384 Scopus citations

Abstract

X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.

Original language	English (US)
Pages (from-to)	1521-1524
Number of pages	4
Journal	Science
Volume	342
Issue number	6165
DOIs	https://doi.org/10.1126/science.1244142
State	Published - 2013

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Liu, W., Wacker, D., Gati, C., Han, G. W., James, D., Wang, D., Nelson, G., Weierstall, U., Katritch, V., Barty, A., Zatsepin, N., Li, D., Messerschmidt, M., Boutet, S., Williams, G. J., Koglin, J. E., Seibert, M. M., Wang, C., Shah, S. T. A., ... Cherezov, V. (2013). Serial femtosecond crystallography of G protein-coupled receptors. Science, 342(6165), 1521-1524. https://doi.org/10.1126/science.1244142

Liu, W, Wacker, D, Gati, C, Han, GW, James, D, Wang, D, Nelson, G, Weierstall, U, Katritch, V, Barty, A, Zatsepin, N, Li, D, Messerschmidt, M, Boutet, S, Williams, GJ, Koglin, JE, Seibert, MM, Wang, C, Shah, STA, Basu, S, Fromme, R, Kupitz, C, Rendek, KN, Grotjohann, I, Fromme, P , Kirian, R, Beyerlein, KR, White, TA, Chapman, HN, Caffrey, M, Spence, J, Stevens, RC & Cherezov, V 2013, 'Serial femtosecond crystallography of G protein-coupled receptors', Science, vol. 342, no. 6165, pp. 1521-1524. https://doi.org/10.1126/science.1244142

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abstract = "X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.",

author = "Wei Liu and Daniel Wacker and Cornelius Gati and Han, {Gye Won} and Daniel James and Dingjie Wang and Garrett Nelson and Uwe Weierstall and Vsevolod Katritch and Anton Barty and Nadia Zatsepin and Dianfan Li and Marc Messerschmidt and S{\'e}bastien Boutet and Williams, {Garth J.} and Koglin, {Jason E.} and Seibert, {M. Marvin} and Chong Wang and Shah, {Syed T A} and Shibom Basu and Raimund Fromme and Christopher Kupitz and Rendek, {Kimberley N.} and Ingo Grotjohann and Petra Fromme and Richard Kirian and Beyerlein, {Kenneth R.} and White, {Thomas A.} and Chapman, {Henry N.} and Martin Caffrey and John Spence and Stevens, {Raymond C.} and Vadim Cherezov",

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AU - Nelson, Garrett

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AU - Seibert, M. Marvin

AU - Wang, Chong

AU - Shah, Syed T A

AU - Basu, Shibom

AU - Fromme, Raimund

AU - Kupitz, Christopher

AU - Rendek, Kimberley N.

AU - Grotjohann, Ingo

AU - Fromme, Petra

AU - Kirian, Richard

AU - Beyerlein, Kenneth R.

AU - White, Thomas A.

AU - Chapman, Henry N.

AU - Caffrey, Martin

AU - Spence, John

AU - Stevens, Raymond C.

AU - Cherezov, Vadim

PY - 2013

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AB - X-ray crystallography of G protein-coupled receptors and other membrane proteins is hampered by difficulties associated with growing sufficiently large crystals that withstand radiation damage and yield high-resolution data at synchrotron sources. We used an x-ray free-electron laser (XFEL) with individual 50-femtosecond-duration x-ray pulses to minimize radiation damage and obtained a high-resolution room-temperature structure of a human serotonin receptor using sub-10-micrometer microcrystals grown in a membrane mimetic matrix known as lipidic cubic phase. Compared with the structure solved by using traditional microcrystallography from cryo-cooled crystals of about two orders of magnitude larger volume, the room-temperature XFEL structure displays a distinct distribution of thermal motions and conformations of residues that likely more accurately represent the receptor structure and dynamics in a cellular environment.

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Serial femtosecond crystallography of G protein-coupled receptors

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Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.

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Serial femtosecond crystallography of G protein-coupled receptors

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Crystal structure of the 5-HT2B receptor solved using serial femtosecond crystallography in lipidic cubic phase.

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