High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Sébastien Boutet; Lukas Lomb; Garth J. Williams; Thomas R M Barends; Andrew Aquila; R. Bruce Doak; Uwe Weierstall; Daniel P. DePonte; Jan Steinbrener; Robert L. Shoeman; Marc Messerschmidt; Anton Barty; Thomas A. White; Stephan Kassemeyer; Richard Kirian; M. Marvin Seibert; Paul A. Montanez; Chris Kenney; Ryan Herbst; Philip Hart; Jack Pines; Gunther Haller; Sol M. Gruner; Hugh T. Philipp; Mark W. Tate; Marianne Hromalik; Lucas J. Koerner; Niels Van Bakel; John Morse; Wilfred Ghonsalves; David Arnlund; Michael J. Bogan; Carl Caleman; Raimund Fromme; Christina Y. Hampton; Mark S. Hunter; Linda C. Johansson; Gergely Katona; Christopher Kupitz; Mengning Liang; Andrew V. Martin; Karol Nass; Lars Redecke; Francesco Stellato; Nicusor Timneanu; Dingjie Wang; Nadia Zatsepin; Donald Schafer; James Defever; Richard Neutze; Petra Fromme; John Spence; Henry N. Chapman; Ilme Schlichting

doi:10.1126/science.1217737

High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Sébastien Boutet, Lukas Lomb, Garth J. Williams, Thomas R M Barends, Andrew Aquila, R. Bruce Doak, Uwe Weierstall, Daniel P. DePonte, Jan Steinbrener, Robert L. Shoeman, Marc Messerschmidt, Anton Barty, Thomas A. White, Stephan Kassemeyer, Richard Kirian, M. Marvin Seibert, Paul A. Montanez, Chris Kenney, Ryan Herbst, Philip HartJack Pines, Gunther Haller, Sol M. Gruner, Hugh T. Philipp, Mark W. Tate, Marianne Hromalik, Lucas J. Koerner, Niels Van Bakel, John Morse, Wilfred Ghonsalves, David Arnlund, Michael J. Bogan, Carl Caleman, Raimund Fromme, Christina Y. Hampton, Mark S. Hunter, Linda C. Johansson, Gergely Katona, Christopher Kupitz, Mengning Liang, Andrew V. Martin, Karol Nass, Lars Redecke, Francesco Stellato, Nicusor Timneanu, Dingjie Wang, Nadia Zatsepin, Donald Schafer, James Defever, Richard Neutze, Petra Fromme, John Spence, Henry N. Chapman, Ilme Schlichting

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

698 Scopus citations

Abstract

Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

Original language	English (US)
Pages (from-to)	362-364
Number of pages	3
Journal	Science
Volume	337
Issue number	6092
DOIs	https://doi.org/10.1126/science.1217737
State	Published - Jul 20 2012

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10.1126/science.1217737

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Boutet, S., Lomb, L., Williams, G. J., Barends, T. R. M., Aquila, A., Doak, R. B., Weierstall, U., DePonte, D. P., Steinbrener, J., Shoeman, R. L., Messerschmidt, M., Barty, A., White, T. A., Kassemeyer, S., Kirian, R., Seibert, M. M., Montanez, P. A., Kenney, C., Herbst, R., ... Schlichting, I. (2012). High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography. Science, 337(6092), 362-364. https://doi.org/10.1126/science.1217737

Boutet, S, Lomb, L, Williams, GJ, Barends, TRM, Aquila, A, Doak, RB, Weierstall, U, DePonte, DP, Steinbrener, J, Shoeman, RL, Messerschmidt, M, Barty, A, White, TA, Kassemeyer, S, Kirian, R, Seibert, MM, Montanez, PA, Kenney, C, Herbst, R, Hart, P, Pines, J, Haller, G, Gruner, SM, Philipp, HT, Tate, MW, Hromalik, M, Koerner, LJ, Van Bakel, N, Morse, J, Ghonsalves, W, Arnlund, D, Bogan, MJ, Caleman, C, Fromme, R, Hampton, CY, Hunter, MS, Johansson, LC, Katona, G, Kupitz, C, Liang, M, Martin, AV, Nass, K, Redecke, L, Stellato, F, Timneanu, N, Wang, D, Zatsepin, N, Schafer, D, Defever, J, Neutze, R, Fromme, P, Spence, J, Chapman, HN & Schlichting, I 2012, 'High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography', Science, vol. 337, no. 6092, pp. 362-364. https://doi.org/10.1126/science.1217737

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abstract = "Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.",

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AU - Boutet, Sébastien

AU - Lomb, Lukas

AU - Williams, Garth J.

AU - Barends, Thomas R M

AU - Aquila, Andrew

AU - Doak, R. Bruce

AU - Weierstall, Uwe

AU - DePonte, Daniel P.

AU - Steinbrener, Jan

AU - Shoeman, Robert L.

AU - Messerschmidt, Marc

AU - Barty, Anton

AU - White, Thomas A.

AU - Kassemeyer, Stephan

AU - Kirian, Richard

AU - Seibert, M. Marvin

AU - Montanez, Paul A.

AU - Kenney, Chris

AU - Herbst, Ryan

AU - Hart, Philip

AU - Pines, Jack

AU - Haller, Gunther

AU - Gruner, Sol M.

AU - Philipp, Hugh T.

AU - Tate, Mark W.

AU - Hromalik, Marianne

AU - Koerner, Lucas J.

AU - Van Bakel, Niels

AU - Morse, John

AU - Ghonsalves, Wilfred

AU - Arnlund, David

AU - Bogan, Michael J.

AU - Caleman, Carl

AU - Fromme, Raimund

AU - Hampton, Christina Y.

AU - Hunter, Mark S.

AU - Johansson, Linda C.

AU - Katona, Gergely

AU - Kupitz, Christopher

AU - Liang, Mengning

AU - Martin, Andrew V.

AU - Nass, Karol

AU - Redecke, Lars

AU - Stellato, Francesco

AU - Timneanu, Nicusor

AU - Wang, Dingjie

AU - Zatsepin, Nadia

AU - Schafer, Donald

AU - Defever, James

AU - Neutze, Richard

AU - Fromme, Petra

AU - Spence, John

AU - Chapman, Henry N.

AU - Schlichting, Ilme

PY - 2012/7/20

Y1 - 2012/7/20

N2 - Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

AB - Structure determination of proteins and other macromolecules has historically required the growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding radiation damage. We applied serial femtosecond crystallography (SFX) using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals (less than 1 micrometer by 1 micrometer by 3 micrometers) of the well-characterized model protein lysozyme. The agreement with synchrotron data demonstrates the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

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SP - 362

EP - 364

JO - Science

JF - Science

IS - 6092

ER -

High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Abstract

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Lysozyme, room-temperature, rotating anode, 0.0026 MGy

Hen egg-white lysozyme solved from 5 fs free-electron laser pulse data

Lysozyme, room temperature, 24 kGy dose

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High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Datasets

Lysozyme, room-temperature, rotating anode, 0.0026 MGy

Hen egg-white lysozyme solved from 5 fs free-electron laser pulse data

Lysozyme, room temperature, 24 kGy dose

Cite this