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 A. 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 A. Zatsepin; Donald Schafer; James Defever; Richard Neutze; Petra Fromme; John C H 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 A. 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 A. Zatsepin, Donald Schafer, James Defever, Richard Neutze, Petra Fromme, John C H Spence, Henry N. Chapman, Ilme Schlichting

^*Corresponding author for this work

Institute of Biochemistry

748 Citations (Scopus)

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
Journal	Science
Volume	337
Issue number	6092
Pages (from-to)	362-364
Number of pages	3
ISSN	0036-8075
DOIs	https://doi.org/10.1126/science.1217737
Publication status	Published - 20.07.2012

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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. A., 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

@article{d3b38e87d4e14b02bb1855cbc30959e8,

title = "High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography",

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.",

author = "S{\'e}bastien Boutet and Lukas Lomb and Williams, \{Garth J.\} and Barends, \{Thomas R M\} and Andrew Aquila and Doak, \{R. Bruce\} and Uwe Weierstall and DePonte, \{Daniel P.\} and Jan Steinbrener and Shoeman, \{Robert L.\} and Marc Messerschmidt and Anton Barty and White, \{Thomas A.\} and Stephan Kassemeyer and Kirian, \{Richard A.\} and Seibert, \{M. Marvin\} and Montanez, \{Paul A.\} and Chris Kenney and Ryan Herbst and Philip Hart and Jack Pines and Gunther Haller and Gruner, \{Sol M.\} and Philipp, \{Hugh T.\} and Tate, \{Mark W.\} and Marianne Hromalik and Koerner, \{Lucas J.\} and \{Van Bakel\}, Niels and John Morse and Wilfred Ghonsalves and David Arnlund and Bogan, \{Michael J.\} and Carl Caleman and Raimund Fromme and Hampton, \{Christina Y.\} and Hunter, \{Mark S.\} and Johansson, \{Linda C.\} and Gergely Katona and Christopher Kupitz and Mengning Liang and Martin, \{Andrew V.\} and Karol Nass and Lars Redecke and Francesco Stellato and Nicusor Timneanu and Dingjie Wang and Zatsepin, \{Nadia A.\} and Donald Schafer and James Defever and Richard Neutze and Petra Fromme and Spence, \{John C H\} and Chapman, \{Henry N.\} and Ilme Schlichting",

year = "2012",

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day = "20",

doi = "10.1126/science.1217737",

language = "English",

volume = "337",

pages = "362--364",

journal = "Science",

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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, RA, 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, NA, Schafer, D, Defever, J, Neutze, R, Fromme, P, Spence, JCH, 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

TY - JOUR

T1 - High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

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 A.

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 A.

AU - Schafer, Donald

AU - Defever, James

AU - Neutze, Richard

AU - Fromme, Petra

AU - Spence, John C H

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.

UR - https://www.scopus.com/pages/publications/84864004802

U2 - 10.1126/science.1217737

DO - 10.1126/science.1217737

M3 - Journal articles

AN - SCOPUS:84864004802

SN - 0036-8075

VL - 337

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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