University Library
  • Login
A gateway to Melbourne's research publications
Minerva Access is the University's Institutional Repository. It aims to collect, preserve, and showcase the intellectual output of staff and students of the University of Melbourne for a global audience.
View Item 
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Microbiology & Immunology
  • Microbiology & Immunology - Research Publications
  • View Item
  • Minerva Access
  • Medicine, Dentistry & Health Sciences
  • Melbourne Medical School
  • Microbiology & Immunology
  • Microbiology & Immunology - Research Publications
  • View Item
JavaScript is disabled for your browser. Some features of this site may not work without it.

    Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8

    Thumbnail
    Citations
    Scopus
    Web of Science
    Altmetric
    12
    13
    Author
    Scott, SA; Holloway, G; Coulson, BS; Szyczew, AJ; Kiefel, MJ; von Itzstein, M; Blanchard, H
    Date
    2005-06-01
    Source Title
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
    Publisher
    INT UNION CRYSTALLOGRAPHY
    University of Melbourne Author/s
    Holloway, Gavan; Coulson, Barbara
    Affiliation
    Microbiology And Immunology
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Scott, S. A., Holloway, G., Coulson, B. S., Szyczew, A. J., Kiefel, M. J., von Itzstein, M. & Blanchard, H. (2005). Crystallization and preliminary X-ray diffraction analysis of the sialic acid-binding domain (VP8*) of porcine rotavirus strain CRW-8. ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 61 (Pt 6), pp.617-620. https://doi.org/10.1107/S1744309105013849.
    Access Status
    Access this item via the Open Access location
    URI
    http://hdl.handle.net/11343/26407
    DOI
    10.1107/S1744309105013849
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952324
    Description

    C1 - Journal Articles Refereed

    Abstract
    Rotavirus recognition and attachment to host cells involves interaction with the spike protein VP4 that projects outwards from the surface of the virus particle. An integral component of these spikes is the VP8* domain, which is implicated in the direct recognition and binding of sialic acid-containing cell-surface carbohydrates and facilitates subsequent invasion by the virus. The expression, purification, crystallization and preliminary X-ray diffraction analysis of VP8* from porcine CRW-8 rotavirus is reported. Diffraction data have been collected to 2.3 A resolution, enabling the determination of the VP8* structure by molecular replacement.
    Keywords
    Medical Virology ; Infectious Diseases

    Export Reference in RIS Format     

    Endnote

    • Click on "Export Reference in RIS Format" and choose "open with... Endnote".

    Refworks

    • Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References


    Collections
    • Minerva Elements Records [45770]
    • Microbiology & Immunology - Research Publications [1555]
    Minerva AccessDepositing Your Work (for University of Melbourne Staff and Students)NewsFAQs

    BrowseCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects
    My AccountLoginRegister
    StatisticsMost Popular ItemsStatistics by CountryMost Popular Authors