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© Research
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

Crystallization of the C-terminal globular domain of avian reovirus fibre.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 01 Jul 2005

van Raaij MJ, Hermo Parrado XL, Guardado Calvo P, Fox GC, Llamas-Saiz AL, Costas C, Martínez-Costas J, Benavente J,

Link to Pubmed [PMID] – 16511119

Acta Crystallogr Sect F Struct Biol Cryst Commun 2005 Jul; 61(Pt 7): 651-4

Avian reovirus fibre, a homotrimer of the sigmaC protein, is responsible for primary host-cell attachment. Using the protease trypsin, a C-terminal sigmaC fragment containing amino acids 156-326 has been generated which was subsequently purified and crystallized. Two different crystal forms were obtained, one grown in the absence of divalent cations and belonging to space group P6(3)22 (unit-cell parameters a = 75.6, c = 243.1 A) and one grown in the presence of either zinc or cadmium sulfate and belonging to space group P321 (unit-cell parameters a = 74.7, c = 74.5 A and a = 73.1, c = 69.9 A for the Zn(II)- and Cd(II)-grown crystals, respectively). The first crystal form diffracted synchrotron radiation to 3.0 A resolution and the second form to 2.2-2.3 A. Its closest related structure, the C-terminal fragment of mammalian reovirus fibre, has only 18% sequence identity and molecular-replacement attempts were unsuccessful. Therefore, a search is under way for suitable heavy-atom derivatives and attempts are being made to grow protein crystals containing selenomethionine instead of methionine.

https://pubmed.ncbi.nlm.nih.gov/16511119