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

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

Apa Reference Singh, A. K., Menéndez-Conejero, R., San Martín, C., & van Raaij, M. J. (2013). Crystallization of the C-terminal domain of the fibre protein from snake adenovirus 1, an atadenovirus. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 69(12), 1374–1379. 10.1107/s1744309113029308
Doi 10.1107/S1744309113029308
Publication Date 29 Nov 2013
Publication Type Article
Researcher Carmen San Martín
Ontology Mutation Analysis and design
Research Groups Structural and physical determinants of complex virus assembly
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