More rapid evaluation of biomacromolecular crystals for diffraction experiments

Arai, Shigeki; Chatake, Toshiyuki; Suzuki, Nobuhiro*; Mizuno, Hiroshi*; Niimura, Nobuo

Acta Crystallographica Section D, 60(6), p.1032 - 1039, 2004/06

https://doi.org/10.1107/S0907444904006559

The parameters used for evaluating biomacromolecular crystal quality (, /(), maximum resolution and mosaicity) strongly depend on the diffraction experimental conditions. In this paper we describe the distinctive features of the relative Wilson plot method, and we show that the overall B-factor obtained from this plot is given as a more appropriate to characterize protein crystals. The relative Wilson plot has been applied to the characterization of crystals of a B-DNA decamer d(CCATTAATGG), and crystals of the proteins DsrD (dissimilatory sulfite reductase D) and hen egg-white lysozyme (HEWL) which we have studied by neutron diffraction. We have found that the crystal qualities of the B-DNA decamer and DsrD significantly depend on the regions of the crystallization phase diagram from which samples were taken. However, in the case of HEWL, crystal quality appears to be independent on the region of the crystallization phase diagram.