Crystallization of the C‐terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3. Issue 10 (8th October 2013)

• Record Type: Journal Article
• Authors: Singh, Abhimanyu K.; Ballmann, Mónika Z.; Benkő, Mária; Harrach, Balázs; van Raaij, Mark J.
• Is Part Of: Acta crystallographica. Volume 69:Issue 10(2013:Oct.)
• Page Start: 1135
• Page End: 1139
• Publication Date: 2013-10-08
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S174430911302397X
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Turkey adenovirus 3 belongs to the genus <italic>Siadenovirus</italic>. Its predicted fibre protein consists of an N‐terminal virus‐attachment domain, a central shaft domain and a head domain at the C‐terminus. The head domain has little sequence identity to known adenovirus fibre head structures. Crystals of the fibre head domain consisting of amino acids 304–454 with an N‐terminal purification tag were produced. Crystals of native and selenomethionine‐derivatized protein belonged to space group <italic>I</italic>23 (unit‐cell parameter 99 Å). They diffracted synchrotron radiation to 2.0 and 2.14 Å resolution, respectively, and are expected to contain one monomer in the asymmetric unit.</p> </abstract>