Mancini E J, Fuller S D
The Structural Biology Programme, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.
Acta Crystallogr D Biol Crystallogr. 2000 Oct;56(Pt 10):1278-87. doi: 10.1107/s0907444900010817.
The recent advances in the resolution obtained by single-particle reconstructions from cryo-electron microscopy (cryo-EM) have led to an increase in studies that combine X-ray crystallographic results with those of electron microscopy (EM). Here, such a combination is described in the determination of the structure of an enveloped animal virus, Semliki Forest virus, at 9 A resolution. The issues of model bias in determination of the structure, the definition of resolution in a single-particle reconstruction, the effect of the correction of the contrast-transfer function on the structure determined and the use of a high-resolution structure of a subunit in the interpretation of the structure of the complex are addressed.
近年来，通过低温电子显微镜（cryo-EM）进行单颗粒重建所获得的分辨率取得了进展，这使得将X射线晶体学结果与电子显微镜（EM）结果相结合的研究有所增加。在此，描述了在9埃分辨率下测定包膜动物病毒——辛德毕斯病毒的结构时的这种结合情况。文中探讨了结构测定中的模型偏差问题、单颗粒重建中分辨率的定义、对比度传递函数校正对所确定结构的影响以及在复合物结构解释中使用亚基的高分辨率结构等问题。
