Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 74, Issue -, Pages 778-786Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2059798318001626
Keywords
neutron crystallography; enzyme mechanisms; deuterons; protons; hydrogen; IMAGINE; neutron diffraction
Funding
- National Science Fundation [0922719]
- Scientific User Facilities Division, Office of Basic Energy Sciences, US Department of Energy
- UT Battelle, LLC [DE-AC05-00OR22725]
- National Science Foundation [0922719]
- National Research Foundation (NRF), South Africa
- USDA NIFA Hatch [1010523]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0922719] Funding Source: National Science Foundation
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Neutron diffraction is exquisitely sensitive to the positions of H atoms in protein crystal structures. IMAGINE is a high-intensity, quasi-Laue neutron crystallography beamline developed at the High Flux Isotope Reactor (HFIR) at Oak Ridge National Laboratory. This state-of-the-art facility for neutron diffraction has enabled detailed structural analysis of macromolecules. IMAGINE is especially suited to resolve individual H atoms in protein structures, enabling neutron protein structures to be determined at or near atomic resolutions from crystals with volumes of less than 1 mm 3 and unit-cell edges of less than 150 angstrom. Beamline features include elliptical focusing mirrors that deliver neutrons into a 2.0 x 3.2 mm focal spot at the sample position, and variable short-and long-wavelength cutoff optics that provide automated exchange between multiple wavelength configurations. This review gives an overview of the IMAGINE beamline at the HFIR, presents examples of the scientific questions being addressed at this beamline, and highlights important findings in enzyme chemistry that have been made using the neutron diffraction capabilities offered by IMAGINE.
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