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

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:
 [1];  [1];  [1]; ORCiD logo [2];  [3];  [3]; ORCiD logo [4]; ORCiD logo [5]
  1. Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States
  2. Janelia Research Campus, Ashburn, United States
  3. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, United States
  4. Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States, Department of Neurology and Neurological Sciences, Howard Hughes Medical Institute, Stanford University, Stanford, United States, Department of Photon Science, Stanford University, Stanford, United States
  5. Department of Molecular and Cellular Physiology, Stanford University, Stanford, United States, Department of Photon Science, Stanford University, Stanford, United States, Department of Structural Biology, Stanford University, Stanford, United States
Publication Date:
Research Org.:
Lawrence Berkeley National Laboratory (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1184051
Alternate Identifier(s):
OSTI ID: 1209798; OSTI ID: 1257268; OSTI ID: 1512179
Grant/Contract Number:  
AC02-05CH11231; GM103393; GM095887; GM102520
Resource Type:
Published Article
Journal Name:
eLife
Additional Journal Information:
Journal Name: eLife Journal Volume: 4; Journal ID: ISSN 2050-084X
Publisher:
eLife Sciences Publications, Ltd.
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; 59 BASIC BIOLOGICAL SCIENCES

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.
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
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.
@article{osti_1184051,
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},
journal = {eLife},
number = ,
volume = 4,
place = {United States},
year = {Tue Mar 17 00:00:00 EDT 2015},
month = {Tue Mar 17 00:00:00 EDT 2015}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record
https://doi.org/10.7554/eLife.05421

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Cited by: 86 works
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