Pierce, J., L. Crow, M. Cuneo, M. Edwards, K.W. Herwig, A. Jennings, A. Jones, et al. “A Prototype System for Dynamically Polarized Neutron Protein Crystallography.” Nuclear Instruments and Methods in Physics Research Section A: Accelerators, Spectrometers, Detectors and Associated Equipment 940 (October 2019): 430–34.
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. 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.
Dynamic Nuclear Polarization Enhanced Neutron Crystallography: Amplifying Hydrogen in Biological Crystals #DNPNMR
From The DNP-NMR Blog:
Dynamic Nuclear Polarization Enhanced Neutron Crystallography: Amplifying Hydrogen in Biological Crystals #DNPNMR
Pierce, Joshua, Matthew J. Cuneo, Anna Jennings, Le Li, Flora Meilleur, Jinkui Zhao, and Dean A.A. Myles. “Dynamic Nuclear Polarization Enhanced Neutron Crystallography: Amplifying Hydrogen in Biological Crystals.” In Methods in Enzymology, 634:153–75. Elsevier, 2020.
https://doi.org/10.1016/bs.mie.2019.11.018.
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Dynamic nuclear polarization enhanced neutron crystallography: Amplifying hydrogen in biological crystals #DNPNMR
From The DNP-NMR Blog:
Dynamic nuclear polarization enhanced neutron crystallography: Amplifying hydrogen in biological crystals #DNPNMR
Pierce, Joshua, Matthew J. Cuneo, Anna Jennings, Le Li, Flora Meilleur, Jinkui Zhao, and Dean A. A. Myles. “Chapter Eight - Dynamic Nuclear Polarization Enhanced Neutron Crystallography: Amplifying Hydrogen in Biological Crystals.” In Methods in Enzymology, edited by Peter C. E. Moody, 634:153–75. Neutron Crystallography in Structural Biology. Academic Press, 2020.
https://doi.org/10.1016/bs.mie.2019.11.018.
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08-07-2020 08:10 PM
Neutron Crystallography Detects Differences in ProteinDynamics: Structure of the PKG II Cyclic Nucleotide Binding Domainin Complex with an Activator
Neutron Crystallography Detects Differences in ProteinDynamics: Structure of the PKG II Cyclic Nucleotide Binding Domainin Complex with an Activator
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00010/20180312/images/medium/bi-2018-00010h_0003.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00010
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/F7_wnrZBMNw
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Lineshape-based polarimetry of dynamically-polarized in solid-state mixtures
From The DNP-NMR Blog:
Lineshape-based polarimetry of dynamically-polarized in solid-state mixtures
Kuzma, N.N., et al., Lineshape-based polarimetry of dynamically-polarized in solid-state mixtures. J. Magn. Reson., 2013. 234(0): p. 90-94.
http://dx.doi.org/10.1016/j.jmr.2013.06.008
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08-09-2013 08:00 PM
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Dynamically committed, uncommitted, and quenched states encoded in protein kinase A revealed by NMR spectroscopy.
Proc Natl Acad Sci U S A. 2011 Apr 6;
Authors: Masterson LR, Shi L, Metcalfe E, Gao J, Taylor SS, Veglia G
Protein kinase A (PKA) is a ubiquitous phosphoryl transferase that mediates hundreds of cell signaling events. During turnover, its catalytic subunit (PKA-C) interconverts between three major conformational states...
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04-08-2011 10:00 AM
[NMR paper] Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe
Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.
Related Articles Distinguishing multiple chemotaxis Y protein conformations with laser-polarized 129Xe NMR.
Protein Sci. 2005 Apr;14(4):848-55
Authors: Lowery TJ, Doucleff M, Ruiz EJ, Rubin SM, Pines A, Wemmer DE
The chemical shift of the (129)Xe NMR signal has been shown to be extremely sensitive to the local environment around the atom and has been used to follow processes such as ligand binding by bacterial periplasmic binding proteins. Here we show...
A prototype system for dynamically polarized neutron protein crystallography #DNPNMR
Linear Mode
