Prof. Dr. Arwen Pearson
Research in my group is focussed on understanding how macromolecular structure leads to function. Biological macromolecules are not static and therefore to understand how they work we need to visualise them with high resolution in both space and time.
We are addressing this challenge in a number of different ways.
Development of new approaches to diffraction data collection.
We recently demonstrated the use of multiplexing to improve the time-resolution of diffraction data collection that we have called Hadamard Time-Resolved Crystallography or HATRX. In collaboration with Thomas Schneider at the EMBL-Hamburg and funded by the BMBF we are now building a new endstation at the EMBL beamlines on PETRA III for these experiments.
Development of new photocages and labels for reaction initiation and probing protein dynamics
Funded by the Hamburg Centre for Ultrafast Imaging and University of Hamburg we have established a synthetic chemistry facility in the Centre for Free Electron Laser Science. Here we are developing photocages with better properties for time-resolved structural measurements. We are also working on getting the photocages into proteins with the aim of making time-resolved experiments as hassle free as possible from the sample preparation point of view.
Using complementary methods to study protein dynamics
We use a combination of crystallography, SAXS, vibrational spectroscopy (IR & THz) and neutron spectroscopy to try to understand how protein motions are linked to function. We work on a range of protein systems, from soluble enzymes to membrane proteins.
We have a long standing interest in understanding and developing ways to mitigate X-radiation damage to samples during diffraction data collection. We lead the ESRF Radiation Damage (RADDAM) BAG that provides beamtime for systematic radiation damage studies to a collaborative team of researchers from across Europe. If you’re interested in joining the BAG drop me a line (arwen.pearson"AT"cfel.de).