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Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3.


ABSTRACT: 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 I23 (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.

SUBMITTER: Singh AK 

PROVIDER: S-EPMC3792674 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3.

Singh Abhimanyu K AK   Ballmann Mónika Z MZ   Benkő Mária M   Harrach Balázs B   van Raaij Mark J MJ  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130928 Pt 10


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 I23 (unit-cell  ...[more]

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