Open AccessCrystallization of the C‐terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3
Author(s) -
Singh Abhimanyu K.,
Ballmann Mónika Z.,
Benkő Mária,
Harrach Balázs,
van Raaij Mark J.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911302397x
Subject(s) - crystallization , head (geology) , terminal (telecommunication) , domain (mathematical analysis) , c terminus , crystallography , materials science , chemistry , biology , biochemistry , engineering , amino acid , paleontology , mathematical analysis , mathematics , organic chemistry , telecommunications
Turkey adenovirus 3 belongs to the genus Siadenovirus . 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 I 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.