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Updated: Aug 24, 2026

An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering
Published on: July 6, 2019
More rapid evaluation of biomacromolecular crystals for diffraction experiments
Shigeki Arai1, Toshiyuki Chatake, Nobuhiro Suzuki
1Neutron Science Research Center, Japan Atomic Energy Research Institute, 2-4 Tokai-mura, Ibaraki-ken, 319-1195, Japan.
Abstract:
The parameters used to evaluate biomacromolecular crystal quality [Rmerge, I/sigma(I), maximum resolution and mosaicity] strongly depend on the experimental diffraction conditions. In this paper, the distinctive features of the relative Wilson plot method are described and it is shown that the overall B factor obtained from this plot is more appropriate for the characterization of protein crystals. The relative Wilson plot has been applied to the characterization of crystals of the B-DNA decamer d(CCATTAATGG) and crystals of the proteins DsrD (dissimilatory sulfite reductase D) and hen egg-white lysozyme (HEWL), which were studied by neutron diffraction. It was found that the crystal quality of the B-DNA decamer and DsrD depended significantly on the regions of the crystallization phase diagram from which the samples were taken. However, in the case of HEWL crystal quality appears to be independent of the region of the crystallization phase diagram.
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