High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Sebastien 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; Institutionen för kemi och molekylärbiologi

doi:10.1126/science.1217737

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High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

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High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Sebastien 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, …

Science (American Association for the Advancement of Science), Vol.337(6092), pp.362-364

07/20/2012

DOI: https://doi.org/10.1126/science.1217737

PMCID: PMC3788707

PMID: 22653729

Abstract

Multidisciplinary Sciences

Science & Technology

Science & Technology - Other Topics

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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Title: High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography
Author/Creator: Sebastien Boutet - Linac Coherent Light Source
Lukas Lomb - Center for Free-Electron Laser Science
Garth J. Williams - Linac Coherent Light Source
Thomas R. M. Barends - Center for Free-Electron Laser Science
Andrew Aquila - Center for Free-Electron Laser Science
R. Bruce Doak - Arizona State University
Uwe Weierstall - Arizona State University
Daniel P. DePonte - Center for Free-Electron Laser Science
Jan Steinbrener - Center for Free-Electron Laser Science
Robert L. Shoeman - Universität Hamburg
Marc Messerschmidt - Linac Coherent Light Source
Anton Barty - Center for Free-Electron Laser Science
Thomas A. White - Center for Free-Electron Laser Science
Stephan Kassemeyer - Center for Free-Electron Laser Science
Richard A. Kirian - Arizona State University
M. Marvin Seibert
Paul A. Montanez - Linac Coherent Light Source
Chris Kenney - SLAC National Accelerator Laboratory
Ryan Herbst - SLAC National Accelerator Laboratory
Philip Hart - SLAC National Accelerator Laboratory
Jack Pines - SLAC National Accelerator Laboratory
Gunther Haller - SLAC National Accelerator Laboratory
Sol M. Gruner - Cornell University
Hugh T. Philipp - Cornell University
Mark W. Tate - Cornell University
Marianne Hromalik - State University of New York at Oswego
Lucas J. Koerner - Johns Hopkins University Applied Physics Laboratory
Niels van Bakel - National Institute for Subatomic Physics
John Morse - European Synchrotron Radiation Facility
Wilfred Ghonsalves - Linac Coherent Light Source
David Arnlund - University of Gothenburg
Michael J. Bogan - SLAC National Accelerator Laboratory
Carl Caleman - Center for Free-Electron Laser Science
Raimund Fromme - Arizona State University
Christina Y. Hampton - SLAC National Accelerator Laboratory
Mark S. Hunter - Arizona State University
Linda C. Johansson - University of Gothenburg
Gergely Katona - University of Gothenburg
Christopher Kupitz - Arizona State University
Mengning Liang - Electron
Andrew V. Martin - Center for Free-Electron Laser Science
Karol Nass - Universität Hamburg
Lars Redecke - University of Lübeck
Francesco Stellato - Center for Free-Electron Laser Science
Nicusor Timneanu - Uppsala University
Dingjie Wang - Arizona State University
Nadia A. Zatsepin - Arizona State University
Donald Schafer - Linac Coherent Light Source
James Defever - Linac Coherent Light Source
Richard Neutze - University of Gothenburg
Petra Fromme - Arizona State University
John C. H. Spence - Arizona State University
Henry N. Chapman - Center for Free-Electron Laser Science
Ilme Schlichting - Center for Free-Electron Laser Science
Institutionen för kemi och molekylärbiologi
Publication Details: Science (American Association for the Advancement of Science), Vol.337(6092), pp.362-364
Publisher: Amer Assoc Advancement Science
Number of pages: 3
Grant note: Max Planck Society; Foundation CELLEX EXC 306 / Deutsche Forschungsgemeinschaft Cluster of Excellence; German Research Foundation (DFG) 0417142; MCB-1021557 / U.S. NSF; National Science Foundation (NSF) 01KX0806; 01KX0807 / German Federal Ministry for Education and Research; Federal Ministry of Education & Research (BMBF) Swedish Foundation for International Cooperation in Research and Higher Education GRANTS:13760191; 1021557 / Direct For Biological Sciences; Div Of Molecular and Cellular Bioscience; National Science Foundation (NSF); NSF - Directorate for Biological Sciences (BIO) DOE, OBES; United States Department of Energy (DOE) 1120997; GRANTS:13615055 / Direct For Biological Sciences; Div Of Molecular and Cellular Bioscience; National Science Foundation (NSF); NSF - Directorate for Biological Sciences (BIO) Swedish Research Council 1R01GM095583 / NIH; United States Department of Health & Human Services; National Institutes of Health (NIH) - USA AMOS program within the Chemical Sciences, Geosciences, and Biosciences Division of the OBES, Office of Science, U.S. DOE; United States Department of Energy (DOE) Hamburg Ministry of Science and Research LCLS Ultrafast Science Instruments (LUSI) project Joachim Herz Stiftung, as part of the Hamburg Initiative for Excellence in Research (LEXI) Hamburg School for Structure and Dynamics in Infection
Academic Unit: Electrical & Computer Engineering
Language: English
Resource Type: Journal article
Record Identifier: 991015164057703691