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Serial femtosecond and serial synchrotron crystallography can yield data of equivalent quality: A systematic comparison

DOI: 10.1126/sciadv.abf1380 DOI Help

Authors: P. Mehrabi (Max Planck Institute for the Structure and Dynamics of Matter; University of Toronto; Ontario Cancer Institute; Center for Free-Electron Laser Science) , R. Bücker (Max Planck Institute for the Structure and Dynamics of Matter; University of Hamburg) , G. Bourenkov (European Molecular Biology Laboratory (EMBL)) , H. M. Ginn (Diamond Light Source) , D. Von Stetten (European Molecular Biology Laboratory (EMBL)) , H. M. Müller-Werkmeister (University of Potsdam) , A. Kuo (University of Toronto) , T. Morizumi (University of Toronto) , B.t. Eger (University of Toronto) , W.-L. Ou (University of Toronto) , S. Oghbaey (University of Toronto) , A. Sarracini (University of Toronto) , J. E. Besaw (University of Toronto) , O. Pare´-Labrosse (Max Planck Institute for the Structure and Dynamics of Matter; University of Toronto) , S. Meier (Universität Hamburg) , H. Schikora (Max Planck Institute for the Structure and Dynamics of Matter) , F. Tellkamp (Max Planck Institute for the Structure and Dynamics of Matter,) , A. Marx (Max Planck Institute for the Structure and Dynamics of Matter; Center for Free-Electron Laser Science) , D. A. Sherrell (Diamond Light Source; Argonne National Laboratory) , D. Axford (Diamond Light Source) , R. I. Owen (Diamond Light Source) , O. P. Ernst (University of Toronto) , E. F. Pai (University of Toronto; Ontario Cancer Institute) , E. C. Schulz (Max Planck Institute for the Structure and Dynamics of Matter; Center for Free-Electron Laser Science) , R. J. D. Miller (Max Planck Institute for the Structure and Dynamics of Matter; Center for Free-Electron Laser Science; University of Toronto; Universität Hamburg)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Science Advances , VOL 7

State: Published (Approved)
Published: March 2021

Open Access Open Access

Abstract: For the two proteins myoglobin and fluoroacetate dehalogenase, 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 micron-sized crystals, the same sample delivery device, and 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 the quality of diffraction data obtained from these samples is linked to the properties of the crystals rather than to the radiation source. Therefore, for other systems with similar properties, time-resolved experiments can be conducted at the radiation source that best matches the desired time resolution.

Subject Areas: Technique Development

Facility: PETRA III; SACLA

Documents:
eabf1380.full.pdf

Discipline Tags:

Life Sciences & Biotech Technique Development - Life Sciences & Biotech

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