| Autor: |
Antoine Sarracini, Olivier Paré-Labrosse, Jessica E. Besaw, Henrike M. Müller-Werkmeister, Takefumi Morizumi, D. von Stetten, R.J.D. Miller, Pedram Mehrabi, H. Schikora, Wei-Lin Ou, Robert Bücker, Robin L. Owen, Emil F. Pai, Friedjof Tellkamp, Helen M. Ginn, Oliver P. Ernst, Gleb Bourenkov, Eric Schulz, A. Kuo, Bryan T. Eger, S. Meier, Andreas Marx, Danny Axford, D.A. Sherrell, Saeed Oghbaey |
| Rok vydání: |
2020 |
| Předmět: |
|
| DOI: |
10.1101/2020.08.21.257170 |
| Popis: |
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. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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