PT  - JOURNAL ARTICLE
AU  - P. Mehrabi
AU  - R. Bücker
AU  - G. Bourenkov
AU  - H.M. Ginn
AU  - D. von Stetten
AU  - H.M. Müller-Werkmeister
AU  - A. Kuo
AU  - T. Morizumi
AU  - B.T. Eger
AU  - W.-L. Ou
AU  - S. Oghbaey
AU  - A. Sarracini
AU  - J.E. Besaw
AU  - O. Paré-Labrosse
AU  - S. Meier
AU  - H. Schikora
AU  - F. Tellkamp
AU  - A. Marx
AU  - D.A. Sherrell
AU  - D. Axford
AU  - R. Owen
AU  - O.P. Ernst
AU  - E.F. Pai
AU  - E.C. Schulz
AU  - R.J.D. Miller
TI  - Serial femtosecond and serial synchrotron crystallography yield data of equivalent quality: a systematic comparison
AID  - 10.1101/2020.08.21.257170
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.08.21.257170
4099  - http://biorxiv.org/content/early/2020/08/22/2020.08.21.257170.short
4100  - http://biorxiv.org/content/early/2020/08/22/2020.08.21.257170.full
AB  - For the two proteins myoglobin (MB) and fluoroacetate dehalogenase (FAcD), we present a systematic comparison of crystallographic diffraction data collected by serial femtosecond (SFX) and serial synchrotron crystallography (SSX). To maximize comparability, we used the same batch of crystals, the same sample delivery device, as well as the same data analysis software. Overall figures of merit indicate that the data of both radiation sources are of equivalent quality. For both proteins reasonable data statistics can be obtained with approximately 5000 room temperature diffraction images irrespective of the radiation source. The direct comparability of SSX and SFX data indicates that diffraction quality is rather linked to the properties of the crystals than to the radiation source. Time-resolved experiments can therefore be conducted at the source that best matches the desired time-resolution.Competing Interest StatementThe authors have declared no competing interest.