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Title: A prototype system for dynamically polarized neutron protein crystallography

Abstract

The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to complement X-ray crystallographic studies using protein crystals. The power of this technique is currently limited by the relative low neutron flux provided by even the most powerful neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow us to use Dynamic Nuclear Polarization to dramatically improve the signal to noise ratio of neutron diffraction data, delivering order of magnitude gains in performance, and enabling measurements of radically smaller crystals of larger protein systems than are possible today. Here, we present a prototype frozen spin system, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor (HFIR). Details of the design and construction will be described, as will the performance of the system offline and during preliminary tests at HFIR.

Authors:
ORCiD logo [1]; ORCiD logo [1]; ORCiD logo [2];  [3]; ORCiD logo [1];  [3];  [1]; ORCiD logo [4]; ORCiD logo [5]; ORCiD logo [1];  [1]; ORCiD logo [6];  [3]; ORCiD logo [7]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); St. Jude's Children Research Hospital, Memphis, TN (United States)
  3. Oak Ridge Associated Univ., Oak Ridge, TN (United States)
  4. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Abilita Bio, Inc., San Diego, CA (United States)
  5. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); North Carolina State Univ., Raleigh, NC (United States)
  6. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); East Tennessee State Univ., Johnson City, TN (United States)
  7. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States); Chinese Academy of Sciences (CAS), Beijing (China)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1531254
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Accepted Manuscript
Journal Name:
Nuclear Instruments and Methods in Physics Research. Section A, Accelerators, Spectrometers, Detectors and Associated Equipment
Additional Journal Information:
Journal Volume: 940; Journal Issue: C; Journal ID: ISSN 0168-9002
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 47 OTHER INSTRUMENTATION; Polarized target; Dynamic nuclear polarization; Protein crystallography; Neutron scattering

Citation Formats

Pierce, Josh, Crow, Jr., Lowell, Cuneo, Matthew J., Edwards, Makayla S., Herwig, Kenneth W., Jennings, Anna D., Jones, Amy, Li, Le, Meilleur, Flora, Myles, Dean A. A., Robertson, Lee, Standaert, Robert F., Wonder, Adam J., and Zhao, J. K. A prototype system for dynamically polarized neutron protein crystallography. United States: N. p., 2019. Web. doi:10.1016/j.nima.2019.06.023.
Pierce, Josh, Crow, Jr., Lowell, Cuneo, Matthew J., Edwards, Makayla S., Herwig, Kenneth W., Jennings, Anna D., Jones, Amy, Li, Le, Meilleur, Flora, Myles, Dean A. A., Robertson, Lee, Standaert, Robert F., Wonder, Adam J., & Zhao, J. K. A prototype system for dynamically polarized neutron protein crystallography. United States. doi:10.1016/j.nima.2019.06.023.
Pierce, Josh, Crow, Jr., Lowell, Cuneo, Matthew J., Edwards, Makayla S., Herwig, Kenneth W., Jennings, Anna D., Jones, Amy, Li, Le, Meilleur, Flora, Myles, Dean A. A., Robertson, Lee, Standaert, Robert F., Wonder, Adam J., and Zhao, J. K. Thu . "A prototype system for dynamically polarized neutron protein crystallography". United States. doi:10.1016/j.nima.2019.06.023.
@article{osti_1531254,
title = {A prototype system for dynamically polarized neutron protein crystallography},
author = {Pierce, Josh and Crow, Jr., Lowell and Cuneo, Matthew J. and Edwards, Makayla S. and Herwig, Kenneth W. and Jennings, Anna D. and Jones, Amy and Li, Le and Meilleur, Flora and Myles, Dean A. A. and Robertson, Lee and Standaert, Robert F. and Wonder, Adam J. and Zhao, J. K.},
abstractNote = {The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to complement X-ray crystallographic studies using protein crystals. The power of this technique is currently limited by the relative low neutron flux provided by even the most powerful neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow us to use Dynamic Nuclear Polarization to dramatically improve the signal to noise ratio of neutron diffraction data, delivering order of magnitude gains in performance, and enabling measurements of radically smaller crystals of larger protein systems than are possible today. Here, we present a prototype frozen spin system, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor (HFIR). Details of the design and construction will be described, as will the performance of the system offline and during preliminary tests at HFIR.},
doi = {10.1016/j.nima.2019.06.023},
journal = {Nuclear Instruments and Methods in Physics Research. Section A, Accelerators, Spectrometers, Detectors and Associated Equipment},
number = C,
volume = 940,
place = {United States},
year = {2019},
month = {6}
}

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This content will become publicly available on June 13, 2020
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