An international team led by LIMS Professor Brian Abbey and Dr Connie Darmanin has developed a new method for tracking the reactions of proteins. The new method, ‘multi-hit serial femtosecond crystallography' or 'multi-hit SFX', could probe biological proteins in a different way, providing scientists with fresh insights into their behaviour. These insights could lead to the development of more effective drugs to combat disease.
The European XFEL flashes on and off up to 27,000 times a second, meaning that a single biological sample can be hit by the X-ray beam twice in less than a microsecond. The first ‘hit’ occurs in the ‘tail’ or weak edge of the beam, meaning that the sample remains intact for the second hit rather than being destroyed by the ultra-intense XFEL radiation. This allows scientists to monitor the reactions of proteins as they move on sub-microsecond time scales. Multi-hit SFX is particularly useful for studying molecules undergoing irreversible processes that cannot be measured using synchrotrons or lab-based X-ray sources.
“Multi-hit SFX potentially opens a novel and unique window into understanding molecular processes, perhaps also for the study of therapeutics,” says Professor Adrian Mancuso, Leading Scientist at the European XFEL and Adjunct Professor at La Trobe University. “This result highlights the unique advantages of the European XFEL’s pulse structure, as well as the success of this collaboration.”
The mult-hit SFX method was published in Nature Communications.
Professor Brian Abbey
Professor Abbey is a Deputy Director at LIMS a Physics professor at La Trobe University and 2022 winner of the ANTSO Eureka Prize for Innovative Use of Technology