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Title
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Crystallization of the C-terminal globular domain of avian reovirus fibre.
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Authors
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M.J.van Raaij,
X.L.Hermo Parrado,
P.Guardado Calvo,
G.C.Fox,
A.L.Llamas-Saiz,
C.Costas,
J.Martínez-Costas,
J.Benavente.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2005,
61,
651-654.
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PubMed id
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Abstract
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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.
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