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

Abhimanyu K. Singh, Mónika Z. Ballmann, M. Benkó, B. Harrach, Mark J. Van Raaij

Research output: Contribution to journalArticle

6 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1135-1139
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number10
DOIs
Publication statusPublished - Oct 2013

Fingerprint

Siadenovirus
adenoviruses
Crystallization
Head
crystallization
proteins
fibers
Fibers
Selenomethionine
Crystals
Proteins
Synchrotron radiation
Viruses
Virus Attachment
Synchrotrons
Purification
Monomers
Adenoviridae
Turkey
Amino Acids

Keywords

  • C-terminal head domain of fibre protein
  • turkey adenovirus 3

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

Crystallization of the C-terminal head domain of the fibre protein from a siadenovirus, turkey adenovirus 3. / Singh, Abhimanyu K.; Ballmann, Mónika Z.; Benkó, M.; Harrach, B.; Van Raaij, Mark J.

In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 69, No. 10, 10.2013, p. 1135-1139.

Research output: Contribution to journalArticle

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