Exploiting subtle structural differences in heavy-atom derivatives for experimental phasing

被引:3
作者
Wang, Jimin [1 ]
Li, Yue [1 ]
Modis, Yorgo [1 ]
机构
[1] Yale Univ, Dept Mol Biophys & Biochem, POB 6666, New Haven, CT 06520 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2014年 / 70卷
基金
美国国家卫生研究院;
关键词
CRYSTAL-STRUCTURE; ANOMALOUS DIFFRACTION; LIGAND-BINDING; RESOLUTION; INCLUSION; INSIGHTS;
D O I
10.1107/S1399004714008943
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Structure determination using the single isomorphous replacement (SIR) or single-wavelength anomalous diffraction (SAD) methods with weak derivatives remains very challenging. In a recent structure determination of glycoprotein E2 from bovine viral diarrhea virus, three isomorphous uranium-derivative data sets were merged to obtain partially interpretable initial experimental maps. Small differences between them were then exploited by treating them as three independent SAD data sets plus three circular pairwise SIR data sets to improve the experimental maps. Here, how such subtle structural differences were exploited for experimental phasing is described in detail. The basis for why this approach works is also provided: the effective resolution of isomorphous signals between highly isomorphous derivatives is often much higher than the effective resolution of the anomalous signals of individual derivative data sets. Hence, the new phasing approaches outlined here will be generally applicable to structure determinations involving weak derivatives.
引用
收藏
页码:1873 / 1883
页数:11
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