De-icing: recovery of diffraction intensities in the presence of ice rings

被引:9
作者
Chapman, Michael S. [1 ]
Somasundaram, Thayumanasamy [2 ]
机构
[1] Oregon Hlth & Sci Univ, Dept Biochem & Mol Biol, Sch Med, Portland, OR 97239 USA
[2] Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 2010年 / 66卷
基金
美国国家卫生研究院;
关键词
LOW-TEMPERATURE; PRESSURE; FORMS;
D O I
10.1107/S0907444910012436
中图分类号
Q5 [生物化学];
学科分类号
070307 [化学生物学];
摘要
Macromolecular structures are routinely determined at cryotemperatures using samples flash-cooled in the presence of cryoprotectants. However, sometimes the best diffraction is obtained under conditions where ice formation is not completely ablated, with the result that characteristic ice rings are superimposed on the macromolecular diffraction. In data processing, the reflections that are most affected by the ice rings are usually excluded. Here, an alternative approach of subtracting the ice diffraction is tested. High completeness can be retained with little adverse effect upon the quality of the integrated data. This offers an alternate strategy when high levels of cryoprotectant lead to loss of crystal quality.
引用
收藏
页码:741 / 744
页数:4
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