Purification and Crystallization of the Yeast Translation Elongation Factor eEF3
Acta crystallographica. Section D, Biological Crystallography
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.
Anderson, Christian Folstead; Anand, Monika; Boesen, Thomas; Van, Lan Bich; Kinzy, Terri Goss; and Andersen, Gregers Rom, "Purification and Crystallization of the Yeast Translation Elongation Factor eEF3" (2004). Faculty Publications – Biological Sciences. 40.