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High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

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

in Animals / Biological and medical sciences / Crystal structure / Crystalline structure / Crystallography / Crystallography, X-Ray - methods / Crystals / Datasets / diffraction data / Electron density / Fundamental and applied biological sciences. Psychology / Lasers / lysozyme / Molecular Biology / Molecular biophysics / Molecules / Molekylärbiologi / Muramidase - chemistry / Muramidase - radiation effects / Nano-technology / nanocrystallography / Nanoteknik / Protein Conformation / protein structure / Proteins / Radiation damage / Radiation dosage / Structure in molecular biology / Synchrotrons / Wave diffraction / X-ray diffraction

2012

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High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

2012

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2012

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Journal Article

High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Weierstall, Uwe,

White, Thomas A.,

Ghonsalves, Wilfred,

Philipp, Hugh T.,

Caleman, Carl,

Neutze, Richard,

Stellato, Francesco,

Kirian, Richard A.,

Lomb, Lukas,

Hart, Philip,

Seibert, M. Marvin,

Gruner, Sol M.,

Martin, Andrew V.,

Kenney, Chris,

Liang, Mengning,

Hampton, Christina Y.,

Arnlund, David,

Katona, Gergely,

Pines, Jack,

Zatsepin, Nadia A.,

Steinbrener, Jan,

Montanez, Paul A.,

Johansson, Linda C.,

Nass, Karol,

Barty, Anton,

Boutet, Sébastien,

DePonte, Daniel P.,

Timneanu, Nicusor,

Koerner, Lucas J.,

van Bakel, Niels,

Fromme, Petra,

Hunter, Mark S.,

Bogan, Michael J.,

Schafer, Donald,

Doak, R. Bruce,

Haller, Gunther,

Wang, Dingjie,

Spence, John C. H.,

Tate, Mark W.,

Shoeman, Robert L.,

Kassemeyer, Stephan,

Schlichting, Ilme,

Hromalik, Marianne,

Defever, James,

Herbst, Ryan,

Chapman, Henry N.,

Aquila, Andrew,

Barends, Thomas R. M.,

Messerschmidt, Marc,

Morse, John,

Williams, Garth J.,

Kupitz, Christopher,

Redecke, Lars,

Fromme, Raimund

2012

Overview

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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Publisher

American Association for the Advancement of Science,The American Association for the Advancement of Science

Subject

Animals

/ Biological and medical sciences

/ Crystal structure

/ Crystalline structure

/ Crystallography

/ Crystallography, X-Ray - methods

/ Crystals