By refining a technique known as cryo-electron microscopy, researchers from Imperial College London and CNRS-Inserm-Strasbourg University have determined how the enzyme RF3 helps prepare the protein-making factory for its next task following disconnection of the newly formed protein strand.

The team's success in capturing the protein-making factory, or ribosome, in action using cryo-electron microscopy will help scientists to begin deciphering the molecular detail of how many antibiotics interfere with the final steps of protein synthesis - an area not currently targeted in antibiotics research.

Professor Marin van Heel of Imperial's Department of Biological Sciences and senior author of the study says:

"Many antibiotics kill bacteria by interfering with their protein-making factories, or ribosomes. But bacteria can often become resistant by mutating their ribosome machinery. Observing ribosomes in action helps us understand which areas of the protein complex evolve such resistance quickly. This information could then be used to develop new antibiotics that target the more stable regions.

"We've used cryo-electron microscopy in a similar way to time lapse footage. It has allowed us to visualise how one cog in a cell's protein manufacturing plant operates. By refining the technique even further we hope to be able to visualise the molecular interactions on an atomic scale. This kind of knowledge has applications across the board when you are trying to work out key factors in diagnosis, treatment or cause of many diseases."

Professor van Heel pioneered cryo-electron microscopy 10 years ago. Since then it has become an essential part of many structural biologists' toolkit. It overcomes the problem of weak image contrast in elect
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Contact: Judith H Moore
j.h.moore@imperial.ac.uk
44-207-594-6702
Imperial College London
25-Feb-2004