Purification and crystallization of the yeast translation elongation factor eEF3

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    Abstract

    A Saccharomyces cerevisiae strain expressing full-length histidine-tagged translation elongation factor 3 (eEF3) as the only form of the protein facilitated purification of the factor for both structural and functional studies. Additionally, an identical full-length form has been successfully expressed in Escherichia coli and a C-terminally truncated form of histidine-tagged eEF3 has been successfully expressed in E. coli and S. cerevisiae. Both forms have been crystallized and crystals of the truncated protein expressed in yeast diffract synchrotron radiation to a maximum resolution of 2.3 A. A density-modified map derived from low-resolution SIRAS phases allows model building.
    Udgivelsesdato: 2004-Jul
    Original languageEnglish
    JournalActa Crystallographica. Section D: Biological Crystallography
    Volume60
    IssuePt 7
    Pages (from-to)1304-7
    Number of pages3
    ISSN0907-4449
    DOIs
    Publication statusPublished - 2004

    Keywords

    • Crystallization
    • Crystallography, X-Ray
    • Escherichia coli
    • Fungal Proteins
    • Peptide Elongation Factors
    • Saccharomyces cerevisiae
    • Saccharomyces cerevisiae Proteins

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