John Helliwell led the development of the world’s first dedicated protein crystallography beamlines; he pioneered the collection of the first broad-band Laue diffraction patterns for protein and virus crystals using synchrotron radiation; he combined biochemistry, spectroscopy, microscopy, protein crystallography and small-angle scattering to study the crustacyanins. He contributed to some of the first developments of synchrotron radiation for phasing based on optimised anomalous scattering and began the investigations of the effects of radiation damage and its potential use for phasing, demonstrating the use of MAD phasing for ab initio structure determination from powder diffraction data. John Helliwell has also served the global crystallographic community through numerous Advisory Committee responsibilities to ensure a speedy and effective growth at as many synchrotrons and neutron facilities as possible; he was the first Chair of the IUCr’s Commission on Synchrotron Radiation. He was president of the European Crystallographic Association (2006–2009) and served as Editor-in-Chief of the IUCr journals (1996–2005).
John Helliwell will receive the award at the 29th European Crystallographic Meeting in Rovinj (Croatia), 23-28 August 2015.
The 8th Max Perutz Prize of the European Crystallographic Association has been awarded to Professor John R. Helliwell, Emeritus Professor of Chemistry, University of Manchester, United Kingdom for his long, generous and fruitful dedication to developing all aspects of the use of synchrotron radiation for crystallography and for his boosting support to global development of synchrotron and neutron facilities. In addition to his pioneering achievements and to the key role that he played in the development of experimental beamlines for structural biology worldwide, he also has been constantly engaged in outreach and dissemination of crystallography to the scientific community.