More rapid evaluation of biomacromolecular crystals for diffraction experiments

被引：16

作者：

Arai, SD

Chatake, T

Suzuki, N

Mizuno, H

Niimura, N

机构：

[1] Japan Atom Energy Res Inst, Neutron Sci Res Ctr, Tokai, Ibaraki 3191195, Japan

[2] Natl Inst Agrobiol Sci, Dept Biochem, Tsukuba, Ibaraki 3058602, Japan

[3] Univ Tsukuba, Inst Appl Biochem, Tsukuba, Ibaraki 3058572, Japan

[4] Ibaraki Univ, Dept Technol, Mito, Ibaraki 3168511, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2004年 / 60卷

关键词：

D O I：

10.1107/S0907444904006559

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The parameters used to evaluate biomacromolecular crystal quality [R-merge, 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 eggwhite 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.

引用

页码：1032 / 1039

页数：8

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