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衍射各向异性与配对精修:白细胞介素10蛋白结合剂H33的晶体结构

Diffraction anisotropy and paired refinement: crystal structure of H33, a protein binder to interleukin 10.

作者信息

Kolenko Petr, Mikulecký Pavel, Pham Phuong Ngoc, Malý Martin, Schneider Bohdan

机构信息

Czech Technical University in Prague, Brehova 7, Prague 115 19, Czech Republic.

Institute of Biotechnology of the Czech Academy of Sciences, Biocev, Průmyslová 595, Vestec 25250, Czech Republic.

出版信息

J Appl Crystallogr. 2023 Jun 16;56(Pt 4):1261-1266. doi: 10.1107/S160057672300479X. eCollection 2023 Aug 1.

Abstract

Binder H33 is a small protein binder engineered by ribosome display to bind human interleukin 10. Crystals of binder H33 display severe diffraction anisotropy. A set of data files with correction for diffraction anisotropy based on different local signal-to-noise ratios was prepared. Paired refinement was used to find the optimal anisotropic high-resolution diffraction limit of the data: 3.13-2.47 Å. The structure of binder H33 belongs to the 2% of crystal structures with the highest solvent content in the Protein Data Bank.

摘要

结合蛋白H33是一种通过核糖体展示技术设计的用于结合人白细胞介素10的小蛋白结合物。结合蛋白H33的晶体表现出严重的衍射各向异性。制备了一组基于不同局部信噪比进行衍射各向异性校正的数据文件。采用配对精修来确定数据的最佳各向异性高分辨率衍射极限:3.13 - 2.47 Å。结合蛋白H33的结构属于蛋白质数据库中溶剂含量最高的2%的晶体结构。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3d02/10405593/9e6088f03dc4/j-56-01261-fig1.jpg

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