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RefNoEC/2003/10
LevelItem
TitleDodson, Eleanor Joy: certificate of election to the Royal Society
CitationEleanor Dodson has made a unique contribution to the mathematical methods of protein crystallography and to their implementation in robust and user-friendly computer programs. As Eleanor Coller, she played a pivotal role in the early application of the rotation and translation functions to an unknown structure, namely insulin. Subsequently she developed these methods for direct structure determination of hagfish insulin and T-state haemoglobin. She introduced the FHLE method of phasing incorporating anomalous-scattering effects and applied it to heavy-atom parameter refinement. She also played a major role in developing methods of regularising molecular structures during crystallographic refinement. More recently, she has exploited maximum-likelihood approaches to computer analysis of crystal structures. She has been the leader in structure analysis of many proteins including TRAP, the tryptophan biosynthesis regulator protein, several lipases, the cell surface receptor CD4, the bacterial peptide transport protein OppA, penicillin acylase and CysB, the cysteine biosynthesis control protein. Beyond all this, her most important role has been as informal leader of a vast effort in coordinating and perfecting publicly-available computer programs which incorporate the accumulated wisdom of protein crystallography. This work, difficult to document in scientific publications, has fuelled the recent explosion of protein structural knowledge, making complex and laborious procedures easily accessible to non-experts.
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