Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals

Uervirojnangkoorn, Monarin; Zeldin, Oliver B.; Lyubimov, Artem Y.; Hattne, Johan; Brewster, Aaron S.; Sauter, Nicholas K.; Brunger, Axel T.; Weis, William I.

doi:10.7554/eLife.05421.001

Title: Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals

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Abstract

There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part due to limitations of data processing methods. We implemented a data processing system based on classical post-refinement techniques, adapted to specific properties of XFEL diffraction data. When applied to XFEL data from three different proteins collected using various sample delivery systems and XFEL beam parameters, our method improved the quality of the diffraction data as well as the resulting refined atomic models and electron density maps. Moreover, the number of observations for a reflection necessary to assemble an accurate data set could be reduced to a few observations. These developments will help expand the applicability of XFEL crystallography to challenging biological systems, including cases where sample is limited.

Authors:

Uervirojnangkoorn, Monarin ^[1]; Zeldin, Oliver B. ^[1]; Lyubimov, Artem Y. ^[1]; Hattne, Johan ^[2]; Brewster, Aaron S. ^[3]; Sauter, Nicholas K. ^[3]; Brunger, Axel T. ^[1]; Weis, William I. ^[1]

Standard Univ., Stanford, CA (United States). Dept. of Molecular and Cellular Physiology.
Janelia Research Campus, Ashburn, VA (United States)
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

Publication Date:: Tue Mar 17 00:00:00 EDT 2015

Research Org.:: Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)

Sponsoring Org.:: USDOE Office of Science (SC)

OSTI Identifier:: 1200901

Grant/Contract Number:: AC02-05CH11231

Resource Type:: Accepted Manuscript

Journal Name:: eLife

Additional Journal Information:: Journal Volume: 4; Journal Issue: e05421; Journal ID: ISSN 2050-084X

Publisher:: eLife Sciences Publications, Ltd.

Country of Publication:: United States

Language:: English

Subject:: 43 PARTICLE ACCELERATORS

Citation Formats


                    Uervirojnangkoorn, Monarin, Zeldin, Oliver B., Lyubimov, Artem Y., Hattne, Johan, Brewster, Aaron S., Sauter, Nicholas K., Brunger, Axel T., and Weis, William I. Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals.  United States: N. p., 2015. 
Web.  doi:10.7554/eLife.05421.001.

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                    Uervirojnangkoorn, Monarin, Zeldin, Oliver B., Lyubimov, Artem Y., Hattne, Johan, Brewster, Aaron S., Sauter, Nicholas K., Brunger, Axel T., & Weis, William I. Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals.  United States.  https://doi.org/10.7554/eLife.05421.001

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                    Uervirojnangkoorn, Monarin, Zeldin, Oliver B., Lyubimov, Artem Y., Hattne, Johan, Brewster, Aaron S., Sauter, Nicholas K., Brunger, Axel T., and Weis, William I. Tue .  
"Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals".  United States.  https://doi.org/10.7554/eLife.05421.001.  https://www.osti.gov/servlets/purl/1200901.

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@article{osti_1200901,

  title        = {Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals},

  author       = {Uervirojnangkoorn, Monarin and Zeldin, Oliver B. and Lyubimov, Artem Y. and Hattne, Johan and Brewster, Aaron S. and Sauter, Nicholas K. and Brunger, Axel T. and Weis, William I.},

  abstractNote = {There is considerable potential for X-ray free electron lasers (XFELs) to enable determination of macromolecular crystal structures that are difficult to solve using current synchrotron sources. Prior XFEL studies often involved the collection of thousands to millions of diffraction images, in part due to limitations of data processing methods. We implemented a data processing system based on classical post-refinement techniques, adapted to specific properties of XFEL diffraction data. When applied to XFEL data from three different proteins collected using various sample delivery systems and XFEL beam parameters, our method improved the quality of the diffraction data as well as the resulting refined atomic models and electron density maps. Moreover, the number of observations for a reflection necessary to assemble an accurate data set could be reduced to a few observations. These developments will help expand the applicability of XFEL crystallography to challenging biological systems, including cases where sample is limited.},

  doi          = {10.7554/eLife.05421.001},

  journal      = {eLife},

  number       = e05421,

  volume       = 4,

  place        = {United States},

  year         = {Tue Mar 17 00:00:00 EDT 2015},

  month        = {Tue Mar 17 00:00:00 EDT 2015}

}

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