Abstract
In their recent commentary in Protein Science, Jaskolski et al. analyzed three randomly picked diffraction data sets from fragment-screening group depositions from the PDB and, based on that, they claimed that such data are principally problematic. We demonstrate here that if such data are treated properly, none of the proclaimed criticisms persist.
| Original language | English |
|---|---|
| Article number | e4391 |
| Pages (from-to) | 1-5 |
| Number of pages | 5 |
| Journal | Protein Science |
| Volume | 31 |
| Issue number | 9 |
| Early online date | 29 Aug 2022 |
| DOIs | |
| Publication status | Published - Sept 2022 |
Bibliographical note
Funding Information:We would like to thank Daren Fearon and Frank von Delft (Diamond Light Source, UK) for providing the map and model files used to generate Figure 1c. We are also grateful for Hans Wienk (NKI Amsterdam, The Netherlands) for critically reading the manuscript and for many textual improvements.
Publisher Copyright:
© 2022 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.
Funding
We would like to thank Daren Fearon and Frank von Delft (Diamond Light Source, UK) for providing the map and model files used to generate Figure 1c. We are also grateful for Hans Wienk (NKI Amsterdam, The Netherlands) for critically reading the manuscript and for many textual improvements.
Keywords
- compositional heterogeneity
- conformational heterogeneity
- fragment-screening
- group depositions
- low-occupancy ligands
- PanDDA
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