Room-temperature X-ray radiation damage to protein crystals using serial crystallography in the EBS context.

Radiation damage is a major limitation in protein crystallography, especially at room temperature (RT), which can lead to incorrect biological interpretation.. Cryo-cooled samples (~100K) have now been used for decades to slow down its progression (~100 fold compared to RT) but such cryo-protection reduces the functionally-relevant conformational heterogeneity of the crystalline sample.
RT data collection recently rejuvenated, through the advent of serial crystallography, in which the X-ray dose deposited on the sample is spread over a large number of microcrystals (typically tens of thousands). In a seminal experiment on ID13, we were able to characterize the progression of radiation damage at RT. However, with the recent EBS upgrade, a 10-fold increase in photon flux density has been obtained on ID13; we therefore propose to reproduce the experiment in these new conditions, to fundamentally understand the mechanism of radiation damage progress at such extreme photon regimes,.