Related Experiment Video
Updated: Aug 14, 2026
09:13
Chromatographic Purification of Highly Active Yeast Ribosomes
Published on: October 24, 2011
Purification and crystallization of the yeast elongation factor eEF2
René Jørgensen1, Anne Carr-Schmid, Pedro A Ortiz
1Institute of Molecular and Structural Biology, University of Aarhus, Gustav Wieds Vej 10C, DK-8000 Aarhus, Denmark.
Summary
Researchers crystallized Saccharomyces cerevisiae elongation factor 2 (eEF2) with GDP, enabling structural and functional studies. This rapid purification method from industrial yeast facilitates further research into eEF2
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Elongation factor 2 (eEF2) is crucial for protein synthesis in eukaryotes.
- Understanding eEF2 structure is key to elucidating its function in translation.
Purpose of the Study:
- To obtain high-quality crystals of Saccharomyces cerevisiae eEF2 in complex with GDP.
- To facilitate structural and functional studies of eEF2.
Main Methods:
- Rapid purification of histidine-tagged eEF2 from industrial yeast.
- Vapour-diffusion technique for crystallization.
- X-ray diffraction analysis of eEF2-GDP crystals.
Main Results:
- Crystals of Saccharomyces cerevisiae eEF2-GDP were successfully obtained.
- The crystals diffract to 2.85 Å resolution and belong to space group P2(1)2(1)2(1).
- A specialized yeast strain enabled efficient purification of functional histidine-tagged eEF2.
Conclusions:
- The developed crystallization method provides a pathway for detailed structural analysis of eEF2.
- This facilitates further investigations into the mechanism of protein elongation.
