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来自蛇腺病毒1(一种腺联病毒)的纤维蛋白C末端结构域的结晶。

Crystallization of the C-terminal domain of the fibre protein from snake adenovirus 1, an atadenovirus.

作者信息

Singh Abhimanyu K, Menéndez-Conejero Rosa, San Martín Carmen, van Raaij Mark J

机构信息

Departamento de Estructura de Macromoléculas, Centro Nacional de Biotecnología (CNB-CSIC), Calle Darwin 3, 28049 Madrid, Spain.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1374-9. doi: 10.1107/S1744309113029308. Epub 2013 Nov 29.

DOI:10.1107/S1744309113029308
PMID:24316834
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3855724/
Abstract

Adenovirus fibre proteins play an important role in determining viral tropism. The C-terminal domain of the fibre protein from snake adenovirus type 1, a member of the Atadenovirus genus, has been expressed, purified and crystallized. Crystals were obtained belonging to space groups P2(1)2(1)2(1) (two different forms), I2(1)3 and F23. The best of these diffracted synchrotron radiation to a resolution of 1.4 Å. As the protein lacks methionines or cysteines, site-directed mutagenesis was performed to change two leucine residues to methionines. Crystals of selenomethionine-derivatized crystals of the I2(1)3 form were also obtained and a multi-wavelength anomalous dispersion data set was collected.

摘要

腺病毒纤维蛋白在决定病毒嗜性方面发挥着重要作用。来自腺病毒属成员蛇腺病毒1型的纤维蛋白的C末端结构域已被表达、纯化和结晶。获得了属于空间群P2(1)2(1)2(1)(两种不同形式)、I2(1)3和F23的晶体。其中最好的晶体将同步辐射衍射到1.4 Å的分辨率。由于该蛋白质缺乏甲硫氨酸或半胱氨酸,因此进行了定点诱变,将两个亮氨酸残基变为甲硫氨酸。还获得了I2(1)3形式的硒代甲硫氨酸衍生晶体,并收集了多波长反常色散数据集。

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