Bilge Tosun, Koç University 

Abstract: 

Many critical steps of translation have never been observed at near-physiological temperatures. Ultrafast and ultrabright X-ray free electron laser (XFEL) pulses will enable us to observe these fast events at an unprecedented temporal and spatial resolution.
Ribosomes are the site of protein synthesis, and prokaryotic ribosomes are a target for more than half of the known antibiotics. These antibiotics block protein synthesis by either interacting with small or the large subunits of the ribosomes. The large ribosomal subunit (50S) is targeted by blockbuster antibiotics such as macrolides and ketolides. In this work, we present the first ambient temperature structure of the large ribosomal subunit (50S) isolated from Thermus Thermophilus, which will enable us to understand the underpinnings of these antibiotic interactions and peptide bond formation at near physiological temperatures. The structural data collected from 50S is a milestone by being one of the largest structures determined at an XFEL, at a record short beamtime of 47 minutes. The application of serial femtosecond X-ray crystallography (SFX) will enable obtaining further structural insights of the ribosome structure and function, and improving our ability to develop new generation antibiotics.

Poster Session Link: https://gather.town/invite?token=0pEoq7VP

If you have any questions for the presenter, please contact them via email: bilgetosun12@gmail.com