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Journal Article

Cryo-electron microscopy structure of yeast Ty retrotransposon virus-like particles

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Tichelaar,  Willem
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Palmer, K. J., Tichelaar, W., Myers, N., Burns, N. R., Butcher, S. J., Kingsman, A. J., et al. (1997). Cryo-electron microscopy structure of yeast Ty retrotransposon virus-like particles. Journal of Virology, 71(9), 6863-6868. Retrieved from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC191967/.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0025-001B-A
Abstract
The virus−like particles (VLPs) produced by the yeast retrotransposon Ty1 are functionally related to retroviral cores. These particles are unusual in that they have variable radif. A paired mass−radius analysis of VLPs by scanning transmission electron microscopy showed that many of these particles form an icosahedral T−number series. Three−dimensional reconstruction to 38−A resolution from cryo−electron micrographs of T = 3 and T = 4 shells revealed that the single structural protein encoded by the TYA gene assembles into spiky shells from trimeric units