Crystallization of the C‐terminal domain of the fibre protein from snake adenovirus 1, an atadenovirus. Issue 12 (1st December 2013)

• Record Type: Journal Article
• Authors: Singh, Abhimanyu K.; Menéndez‐Conejero, Rosa; San Martín, Carmen; van Raaij, Mark J.
• Is Part Of: Acta crystallographica. Volume 69:Issue 12(2013:Dec.)
• Page Start: 1374
• Page End: 1379
• Publication Date: 2013-12-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113029308
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Atadenovirus</italic> genus, has been expressed, purified and crystallized. Crystals were obtained belonging to space groups <italic>P</italic>2₁2₁2₁ (two different forms), <italic>I</italic>2₁3 and <italic>F</italic>23. 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 <italic>I</italic>2₁3 form were also obtained and a multi‐wavelength anomalous dispersion data set was collected.</p> </abstract>