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Cryo-EM targets in CASP14
Proteins: Structure, Function, and Bioinformatics ( IF 3.2 ) Pub Date : 2021-08-16 , DOI: 10.1002/prot.26216
Tristan Cragnolini 1 , Andriy Kryshtafovych 2 , Maya Topf 3
Affiliation  

Structures of seven CASP14 targets were determined using cryo-electron microscopy (cryo-EM) technique with resolution between 2.1 and 3.8 Å. We provide an evaluation of the submitted models versus the experimental data (cryo-EM density maps) and experimental reference structures built into the maps. The accuracy of models is measured in terms of coordinate-to-density and coordinate-to-coordinate fit. A-posteriori refinement of the most accurate models in their corresponding cryo-EM density resulted in structures that are close to the reference structure, including some regions with better fit to the density. Regions that were found to be less “refineable” correlate well with regions of high diversity between the CASP models and low goodness-of-fit to density in the reference structure.

中文翻译:

CASP14 中的冷冻电镜目标

使用分辨率在 2.1 和 3.8 Å 之间的低温电子显微镜 (cryo-EM) 技术确定了七个 CASP14 靶标的结构。我们对提交的模型与实验数据(低温电磁密度图)和图中内置的实验参考结构进行了评估。模型的准确性是根据坐标到密度和坐标到坐标的拟合来衡量的。在相应的低温电磁密度中对最精确模型进行后验优化,得到的结构接近参考结构,包括一些更适合密度的区域。被发现不太“可精炼”的区域与 CASP 模型之间的高多样性区域和参考结构中与密度的低拟合优度区域相关性很好。
更新日期:2021-08-16
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