ArticleActa crystallographica. Section F, Structural biology and crystallization communications2005
Crystallization of the C-terminal globular domain of avian reovirus fibre.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 7 citations in OpenAlex.
- Crystallization of the C-terminal domain of the bacteriophage T7 fibre protein gp17.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Sequence and phylogenetic analysis of the S1 genome segment of turkey-origin reoviruses.Virus genes · 2007Article
- Crystallization of the C-terminal head domain of the avian adenovirus CELO long fibre.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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