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Re-evaluation of protein neutron crystallography with and without X-ray/neutron joint refinement

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The crystallographic structure of a bacterial copper amine oxidase was determined solely using neutron diffraction data at 1.72 Å resolution. Although the neutron scattering length densities thus obtained were sufficient to… Click to show full abstract

The crystallographic structure of a bacterial copper amine oxidase was determined solely using neutron diffraction data at 1.72 Å resolution. Although the neutron scattering length densities thus obtained were sufficient to determine the locations of all atoms, including H and D atoms, it was confirmed that joint refinement with high-resolution X-ray diffraction data provided more accurate structural features that were not visible in the structure refined from the neutron data alone.

Keywords: ray; evaluation protein; protein neutron; neutron; joint refinement

Journal Title: IUCrJ
Year Published: 2022

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