Research Investigating the molecular basis of cataract formation using time-resolved crystallography

This project will involve the application of state-of-the-art X-ray crystallographic techniques, developed by the PI, to investigate the molecular processes that lead to the formation of cataracts, the leading cause of blindness worldwide.

Using time-resolved X-ray crystallography to make molecular movies allows us to observe the structural changes that occur when proteins and enzymes undergo their natural functions.

This can help us to design new drugs and materials, improve the properties of biological molecules and more fundamentally, understand the relationship between protein structure and function.

This information can even be used to enhance computer simulations, used to predict the effect of changing the protein sequence or determining the interaction of novel drug targets.

Time-resolved crystallography will allow us to directly observe the effect of UV light on the proteins contained within the eye lens.

This will give unique insight into the molecular basis of UV induced cataract formation, and provide a way to investigate new drugs for the prevention and treatment of cataracts.

With the advent of free-electron laser X-ray sources, time-resolved crystallography has become the state-of-the-art for the experimental determination of protein dynamics.

This project will use a unique method developed by the PI (Hadamard time-resolved crystallography, HATRX) which has been cited as a significant contribution to the emerging field of multiplexing crystallography.