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Title: 7 Å Resolution in Protein 2-Dimentional-Crystal X-Ray Diffraction at Linac Coherent Light Source

Abstract

Membrane proteins arranged as two-dimensional (2D) crystals in the lipid en- vironment provide close-to-physiological structural information, which is essential for understanding the molecular mechanisms of protein function. X-ray diffraction from individual 2D crystals did not represent a suitable investigation tool because of radiation damage. The recent availability of ultrashort pulses from X-ray Free Electron Lasers (X-FELs) has now provided a mean to outrun the damage. Here we report on measurements performed at the LCLS X-FEL on bacteriorhodopsin 2D crystals mounted on a solid support and kept at room temperature. By merg- ing data from about a dozen of single crystal diffraction images, we unambiguously identified the diffraction peaks to a resolution of 7 °A, thus improving the observable resolution with respect to that achievable from a single pattern alone. This indicates that a larger dataset will allow for reliable quantification of peak intensities, and in turn a corresponding increase of resolution. The presented results pave the way to further X-FEL studies on 2D crystals, which may include pump-probe experiments at subpicosecond time resolution.

Authors:
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Publication Date:
Research Org.:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
Sponsoring Org.:
USDOE
OSTI Identifier:
1134521
Report Number(s):
PNNL-SA-100713
48143
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Journal Name:
Philosophical Transactions of the Royal Society of London Series B, Biological Sciences, 369(1647):Article No. 20130500
Additional Journal Information:
Journal Name: Philosophical Transactions of the Royal Society of London Series B, Biological Sciences, 369(1647):Article No. 20130500
Country of Publication:
United States
Language:
English
Subject:
Environmental Molecular Sciences Laboratory

Citation Formats

Pedrini, Bill, Tsai, Ching-Ju, Capitani, Guido, Padeste, Celestino, Hunter, Mark, Zatsepin, Nadia A., Barty, Anton, Benner, Henry, Boutet, Sebastien, Feld, Geoffrey K., Hau-Riege, Stefan, Kirian, Rick, Kupitz, Christopher, Messerschmidt, Marc, Ogren, John I., Pardini, Tommaso, Segelke, Brent, Williams, Garth J., Spence, John C., Abela, Rafael, Coleman, Matthew A., Evans, James E., Schertler, Gebhard, Frank, Matthias, and Li, Xiao-Dan. 7 Å Resolution in Protein 2-Dimentional-Crystal X-Ray Diffraction at Linac Coherent Light Source. United States: N. p., 2014. Web. doi:10.1098/rstb.2013.0500.
Pedrini, Bill, Tsai, Ching-Ju, Capitani, Guido, Padeste, Celestino, Hunter, Mark, Zatsepin, Nadia A., Barty, Anton, Benner, Henry, Boutet, Sebastien, Feld, Geoffrey K., Hau-Riege, Stefan, Kirian, Rick, Kupitz, Christopher, Messerschmidt, Marc, Ogren, John I., Pardini, Tommaso, Segelke, Brent, Williams, Garth J., Spence, John C., Abela, Rafael, Coleman, Matthew A., Evans, James E., Schertler, Gebhard, Frank, Matthias, & Li, Xiao-Dan. 7 Å Resolution in Protein 2-Dimentional-Crystal X-Ray Diffraction at Linac Coherent Light Source. United States. https://doi.org/10.1098/rstb.2013.0500
Pedrini, Bill, Tsai, Ching-Ju, Capitani, Guido, Padeste, Celestino, Hunter, Mark, Zatsepin, Nadia A., Barty, Anton, Benner, Henry, Boutet, Sebastien, Feld, Geoffrey K., Hau-Riege, Stefan, Kirian, Rick, Kupitz, Christopher, Messerschmidt, Marc, Ogren, John I., Pardini, Tommaso, Segelke, Brent, Williams, Garth J., Spence, John C., Abela, Rafael, Coleman, Matthew A., Evans, James E., Schertler, Gebhard, Frank, Matthias, and Li, Xiao-Dan. 2014. "7 Å Resolution in Protein 2-Dimentional-Crystal X-Ray Diffraction at Linac Coherent Light Source". United States. https://doi.org/10.1098/rstb.2013.0500.
@article{osti_1134521,
title = {7 Å Resolution in Protein 2-Dimentional-Crystal X-Ray Diffraction at Linac Coherent Light Source},
author = {Pedrini, Bill and Tsai, Ching-Ju and Capitani, Guido and Padeste, Celestino and Hunter, Mark and Zatsepin, Nadia A. and Barty, Anton and Benner, Henry and Boutet, Sebastien and Feld, Geoffrey K. and Hau-Riege, Stefan and Kirian, Rick and Kupitz, Christopher and Messerschmidt, Marc and Ogren, John I. and Pardini, Tommaso and Segelke, Brent and Williams, Garth J. and Spence, John C. and Abela, Rafael and Coleman, Matthew A. and Evans, James E. and Schertler, Gebhard and Frank, Matthias and Li, Xiao-Dan},
abstractNote = {Membrane proteins arranged as two-dimensional (2D) crystals in the lipid en- vironment provide close-to-physiological structural information, which is essential for understanding the molecular mechanisms of protein function. X-ray diffraction from individual 2D crystals did not represent a suitable investigation tool because of radiation damage. The recent availability of ultrashort pulses from X-ray Free Electron Lasers (X-FELs) has now provided a mean to outrun the damage. Here we report on measurements performed at the LCLS X-FEL on bacteriorhodopsin 2D crystals mounted on a solid support and kept at room temperature. By merg- ing data from about a dozen of single crystal diffraction images, we unambiguously identified the diffraction peaks to a resolution of 7 °A, thus improving the observable resolution with respect to that achievable from a single pattern alone. This indicates that a larger dataset will allow for reliable quantification of peak intensities, and in turn a corresponding increase of resolution. The presented results pave the way to further X-FEL studies on 2D crystals, which may include pump-probe experiments at subpicosecond time resolution.},
doi = {10.1098/rstb.2013.0500},
url = {https://www.osti.gov/biblio/1134521}, journal = {Philosophical Transactions of the Royal Society of London Series B, Biological Sciences, 369(1647):Article No. 20130500},
number = ,
volume = ,
place = {United States},
year = {Mon Jun 09 00:00:00 EDT 2014},
month = {Mon Jun 09 00:00:00 EDT 2014}
}