1199531_Kirkwood,H.J_2022.pdf (1 MB)
A multi-million image Serial Femtosecond Crystallography dataset collected at the European XFEL
journal contributionposted on 2022-05-09, 07:03 authored by HJ Kirkwood, R de Wijn, G Mills, R Letrun, M Kloos, M Vakili, M Karnevskiy, K Ahmed, RJ Bean, J Bielecki, F Dall’Antonia, Y Kim, C Kim, J Koliyadu, A Round, T Sato, M Sikorski, P Vagovič, J Sztuk-Dambietz, Adrian MancusoAdrian Mancuso
Serial femtosecond crystallography is a rapidly developing method for determining the structure of biomolecules for samples which have proven challenging with conventional X-ray crystallography, such as for membrane proteins and microcrystals, or for time-resolved studies. The European XFEL, the first high repetition rate hard X-ray free electron laser, provides the ability to record diffraction data at more than an order of magnitude faster than previously achievable, putting increased demand on sample delivery and data processing. This work describes a publicly available serial femtosecond crystallography dataset collected at the SPB/SFX instrument at the European XFEL. This dataset contains information suitable for algorithmic development for detector calibration, image classification and structure determination, as well as testing and training for future users of the European XFEL and other XFELs.