Welcome to the Ribosome Crystallography Group

Our group takes a multi-disciplinary approach, using X-ray crystallography, Nuclear Magnetic Resonance (NMR), Mass Spectrometry (MS) and cryo-electron microscopy (EM), to understand how the ribosome is regulated in the cell.

Our projects encompass the factors involved in the regulation of ribosomal subunit assembly, the inactivation of the ribosome by (i) antibiotics or (ii) under stress conditions by protein factor(s), and the regulation of translation through (i) binding of factors, (ii) interaction of the nascent polypeptide chain with the ribosomal tunnel or (iii) via modulating the composition of the ribosome itself.

Cells 50S Crystals X-Ray Diffraction Ligand bound EM-70S Model X-Ray-30S Model

The Ribosome:

In every organism, translation of the genetic code into functional proteins is performed on the ribosome, a macromolecular machine of more than 2.3 MDa. In the eubacteria Escherichia coli the ribosome is assembled from at least 55 different proteins and three RNA molecules (23S, 16S and 5S rRNA). This intact species is termed the 70S ribosome and is made up of two distinct components, the 30S and 50S subunits.

The high-resolution structures of the small and large ribosome subunit, in the past few years have revolutionized our understanding of ribosome structure and function.

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