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High resolution crystal structure of the ribosome opens way for exciting research

The Biochemical Society’s Heatley Medal ‘for exceptional work that makes biochemistry widely accessible and usable’ has been won by Venki Ramakrishnan (MRC LMB, Cambridge) for his seminal work on the structure and function of the bacterial ribosome and for his work on the organization of the key components of eukaryotic chromatin and the enzymes that modify its state.

This work has explained, for the first time, how specificity in translation is achieved that is so much greater than that expected from the hydrogen bonding between cognate codons of tRNA and messenger RNA alone.

Dr Norman Heatley, in whose name the Award is given, is known as the scientist who overcame wartime shortages to make the production of penicillin possible and his role in paving the way for mass production was well documented in his obituaries early in 2004.

Professor Venki Ramakrishnan studied for his PhD at Ohio University and continued his research career at Yale University with Peter Moore, where he mapped the location of protein subunits within the ribosome assembly. He then established his own laboratory at Oak Ridge National Laboratory, and then at Brookhaven National Laboratory, where he continued work on ribosomal proteins and initiated work on chromatin proteins. While on sabbatical at the MRC LMB, Venki solved the crystal structure of the globular domain of the histone H5 protein that is associated with compacted chromatin. In 1995 he moved from Utah to the MRC Laboratory of Molecular Biology, Cambridge where he is now Group Leader of the Structural Studies Division.

Mark Burgess | alfa
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