I am Professor of Molecular Biophysics and a Nicholas Kurti Senior Research Fellow in Macromolecular Crystallography.
My group's research is aimed at developing new techniques for protein crystallography which will enable larger and more complex molecules to be studied. We have been heavily involved with establishing methods for collecting X-ray data with the crystal held at cryotemperatures (usually 100 K) which significantly reduces (around a factor of 70 times) the rate of radiation damage to the crystal. We are currently working on understanding the effects of this damage on the biological information that is obtained from 3-D structures, and trying to find experimental strategies to mitigate it.
Proteins often contain metals vital to their function. Using the technique of Proton Induced X-ray Emission (microPIXE) we have established a way to unambiguously determine the elemental composition of liquid and crystalline proteins and identify the bound metals. This is now being developed into a high throughput technique which will allow much more detailed studies of metal binding to biological samples.
We also carry out structural studies which have focussed so far on the 3-D structures of viral (influenza) and bacterial neuraminidases, and more recently on parts of human fibronectin and Mycobacterium Tuberculosis.