Published January 9, 2022
| Version v1
Dataset
Open
Large-scale conformational changes of FhaC provide insights into the two-partner secretion mechanism
Creators
- 1. Laboratoire Avancé de Spectroscopie pour les Interactions, la Réactivité et l'Environnement (LASIRE), UMR CNRS 8516, Université de Lille, Lille, France
- 2. Thermo Fisher Scientific, Eindhoven, The Netherlands
- 3. Calixar, Lyon, France
- 4. Laboratoire de Spectrométrie de Masse BioOrganique, Université de Strasbourg, CNRS, IPHC UMR 7178, Strasbourg, France
- 5. CNRS, INSERM, Institut Pasteur de Lille, U1019-UMR9017-CIIL-Center for Infection and Immunity of Lille, Lille, France
- 6. ERL 9002 CNRS Biologie Structurale Intégrative, UMR INSERM 1167, Université de Lille, Lille, France
- 7. Institut für Organische Chemie, Gottfried Wilhelm Leibniz Universität Hannover, Hannover, Germany
- 8. Astbury Centre for Structural Molecular Biology and the School of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom
- 9. Bruker Switzerland AG, Fällanden, Switzerlan
Description
This dataset contains raw and processed data and analyses related to the manuscript "Large-scale conformational changes of FhaC provide insights into the two-partner secretion mechanism" by the authors. A preprint of this manuscript is available on bioRxiv (https://doi.org/10.1101/2021.11.09.467682).
Notes
Files
FhaC_EPRdata.zip
Additional details
Related works
- Is source of
- Journal article: 10.1101/2021.11.09.467682 (DOI)
Funding
- OPEN_BAR – Fonctionally relevant conformations of the protein transporter FhaC: probing the lateral opening of a beta barrel in a biological membrane ANR-17-CE11-0043
- Agence Nationale de la Recherche