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      Neutron protein crystallography: A complementary tool for locating hydrogens in proteins.

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          Abstract

          Neutron protein crystallography is a powerful tool for investigating protein chemistry because it directly locates hydrogen atom positions in a protein structure. The visibility of hydrogen and deuterium atoms arises from the strong interaction of neutrons with the nuclei of these isotopes. Positions can be unambiguously assigned from diffraction at resolutions typical of protein crystals. Neutrons have the additional benefit to structural biology of not inducing radiation damage in protein crystals. The same crystal could be measured multiple times for parametric studies. Here, we review the basic principles of neutron protein crystallography. The information that can be gained from a neutron structure is presented in balance with practical considerations. Methods to produce isotopically-substituted proteins and to grow large crystals are provided in the context of neutron structures reported in the literature. Available instruments for data collection and software for data processing and structure refinement are described along with technique-specific strategies including joint X-ray/neutron structure refinement. Examples are given to illustrate, ultimately, the unique scientific value of neutron protein crystal structures.

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          Author and article information

          Journal
          Arch. Biochem. Biophys.
          Archives of biochemistry and biophysics
          Elsevier BV
          1096-0384
          0003-9861
          Jul 15 2016
          : 602
          Affiliations
          [1 ] Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA; Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA.
          [2 ] Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, NC 27695, USA; Neutron Sciences Directorate, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA. Electronic address: fmeille@ncsu.edu.
          Article
          S0003-9861(15)30104-1
          10.1016/j.abb.2015.11.033
          26592456

          Water, Crystallography, Enzyme, Hydrogen, Neutron, Protonation

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