Dynamic nuclear polarization for neutron protein crystallography

Josh Pierce

Dynamic nuclear polarization for neutron protein crystallography

Josh Pierce

HFIR Low Temperature and Magnets

Research output: Contribution to journal › Conference article › peer-review

1 Scopus citations

Abstract

The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to study protein structure. This technique is currently limited by the relative low neutron flux provided by even the most modern neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow Dynamic Nuclear Polarization to dramatically improve the sensitivity of protein structure measurements. This will enable the use of substantially smaller protein crystals, allowing structure measurements which are currently impossible. We present a proof of concept frozen spin target, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor. The results of the first test on the neutron beam will be discussed, as will planned upgrades to the system.

Original language	English
Journal	Proceedings of Science
Volume	324
State	Published - 2017
Event	17th International Workshop on Polarized Sources, Targets and Polarimetry, PSTP 2017 - Daejeon, Korea, Republic of Duration: Oct 16 2017 → Oct 20 2017

Funding

Research sponsored by the Laboratory Directed Research and Development Program of Oak Ridge National Laboratory, managed by UT-Battelle, LLC, for the U. S. Department of Energy. This research was done in collaboration with the members of the DyPol LDRD team. The construction and installation of the IMAGINE beam line was partly supported by NSF grant CHE-0922719.

Funders	Funder number
U. S. Department of Energy
UT-Battelle
National Science Foundation	CHE-0922719
U.S. Department of Energy
National Sleep Foundation
Oak Ridge National Laboratory
Laboratory Directed Research and Development

Cite this

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title = "Dynamic nuclear polarization for neutron protein crystallography",

abstract = "The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to study protein structure. This technique is currently limited by the relative low neutron flux provided by even the most modern neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow Dynamic Nuclear Polarization to dramatically improve the sensitivity of protein structure measurements. This will enable the use of substantially smaller protein crystals, allowing structure measurements which are currently impossible. We present a proof of concept frozen spin target, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor. The results of the first test on the neutron beam will be discussed, as will planned upgrades to the system.",

author = "Josh Pierce",

note = "Publisher Copyright: {\textcopyright} Copyright owned by the author(s) under the terms of the Creative Commons.; 17th International Workshop on Polarized Sources, Targets and Polarimetry, PSTP 2017 ; Conference date: 16-10-2017 Through 20-10-2017",

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AU - Pierce, Josh

N1 - Publisher Copyright: © Copyright owned by the author(s) under the terms of the Creative Commons.

PY - 2017

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N2 - The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to study protein structure. This technique is currently limited by the relative low neutron flux provided by even the most modern neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow Dynamic Nuclear Polarization to dramatically improve the sensitivity of protein structure measurements. This will enable the use of substantially smaller protein crystals, allowing structure measurements which are currently impossible. We present a proof of concept frozen spin target, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor. The results of the first test on the neutron beam will be discussed, as will planned upgrades to the system.

AB - The sensitivity of Neutron Macromolecular Crystallography to the presence of hydrogen makes it a powerful tool to study protein structure. This technique is currently limited by the relative low neutron flux provided by even the most modern neutron sources. The strong polarization dependence of the neutron scattering cross section of hydrogen will allow Dynamic Nuclear Polarization to dramatically improve the sensitivity of protein structure measurements. This will enable the use of substantially smaller protein crystals, allowing structure measurements which are currently impossible. We present a proof of concept frozen spin target, built at Oak Ridge National Laboratory to polarize single protein crystals on the IMAGINE beamline at the High Flux Isotope Reactor. The results of the first test on the neutron beam will be discussed, as will planned upgrades to the system.

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M3 - Conference article

AN - SCOPUS:85073554076

SN - 1824-8039

VL - 324

JO - Proceedings of Science

JF - Proceedings of Science

T2 - 17th International Workshop on Polarized Sources, Targets and Polarimetry, PSTP 2017

Y2 - 16 October 2017 through 20 October 2017

ER -

Dynamic nuclear polarization for neutron protein crystallography

Abstract

Funding

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