X-ray crystallography has been tremendously successful over many decades in defining the structures of proteins, leading to major advances in our understanding of cellular functions.
Proteins are highly dynamic molecules that adopt a range of conformations while carrying out their functions. However, crystal structures typically represent only the time-averaged structure of a cryogenically-preserved crystalline protein, and essential dynamic information is lost.
To exacerbate this, protein structures at 100 K may differ significantly from those adopted under closer to physiological conditions, while the ionising X-ray radiation used to determine the structures is a destructive probe that causes chemical changes (radiation damage) to the protein.
Dr Mike Hough will describe new approaches being developed at Essex, in partnership with advanced light sources, to address the above issues and work towards producing time-resolved structures under non-cryogenic conditions, that are free of the effects of radiation damage.