ACCURACY OF REFINED PROTEIN STRUCTURES .2. COMPARISON OF 4 INDEPENDENTLY REFINED MODELS OF HUMAN INTERLEUKIN-1-BETA

被引:41
作者
OHLENDORF, DH [1 ]
机构
[1] DUPONT CO INC,DEPT CENT RES & DEV,EXPTL STN,WILMINGTON,DE 19880
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1994年 / 50卷
关键词
D O I
10.1107/S0907444994002659
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
To assess the accuracy of refined structures, a comparison was made using independently determined structures of the same protein in the same crystal form. The models were re-refined against a common data set to minimize the effects of different data and different refinement protocols. The process did not converge to a single model. Rather the structures differed from each other by 0.84 Angstrom which was roughly three times that predicted by a Luzzati analysis [Luzzati (1952). Acta Cryst. 5, 802-810]. The individual structures are equally valid and at least partially independent as evidenced by a reduction of the R factor by 0.013 when a simple linear combination is used. Only 29 solvent molecules were common to all four models.
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页码:808 / 812
页数:5
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