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Christian Brix Folsted Andersen

Purification and crystallization of the yeast translation elongation factor eEF3

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  • Department of Molecular Biology
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
IssuePt 7
Pages (from-to)1304-7
Number of pages3
Publication statusPublished - 2004

    Research areas

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

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