Room-temperature serial crystallography
Room-temperature serial crystallography data are of comparable quality and have several advantages over the data collected at cryo-temperatures. In particular, room-temperature structure determination is more physiologically relevant, enables time-resolved investigations of protein kinetics, and reduces crystal handling. This kind of data collection scheme can be performed at XFEL sources, but due to the scarcity of the beamtime available at XFEL facilities, serial data collection is now done also at synchrotron sources in a routine manner. Serial crystallography approach requires continuous replenishment of the sample, as most of the time only one diffraction pattern is obtained from a single crystal. This requires development of novel and versatile sample delivery methods and work on improved data processing pipelines. As a part of the XFEL-Hub team I am involved in establishing serial data collection schemes at Diamond, e.g. high-viscosity extruder system, which is also regularly used at SACLA and LCLS XFEL facilities. By that we enable users to test their samples in an XFEL-like environment (for example before submitting their XFEL beamtime proposals) or to collect complete room-temperature datasets from microcrystals.
Synthesis of cyclic nucleotides
My work at the Research Complex at Harwell is focused on structural analysis of proteins involved in the synthesis of cyclic and di-cyclic nucleotides. I am interested in time-resolved X-ray analysis of the reaction catalyzed by these classes of enzymes, in particular where synthesis of the second messenger is linked to a photoinduced reaction cycle of the internal chromophore in the sensory domain.