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History
- May 17, 2022.
Copyright
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
Author Information
- Jan Steinkühler1,*,
- Charlotte H. Abrahamson2,
- Jaime Agudo-Canalejo3,
- Ramin Golestanian3,4,
- Danielle Tullman-Ercek2,5,6,* and
- Neha P. Kamat1,5,6,*
- 1Department of Biomedical Engineering, Northwestern University, Evanston, IL 60657
- 2Department of Chemical and Biological Engineering, Northwestern University, 9 Evanston, Illinois, USA
- 3Department of Living Matter Physics, Max Planck Institute for Dynamics and Self-Organization, D-37077 Göttingen, Germany
- 4Rudolf Peierls Centre for Theoretical Physics, University of Oxford, Oxford OX1 3PU, United Kingdom
- 5Center for Synthetic Biology, Northwestern University, Evanston, IL 60657
- 6Chemistry of Life Processes, Evanston, IL 60657
- ↵*Corresponding authors: nkamat{at}northwestern.edu;ercek{at}northwestern.edu; jan.steinkuehler{at}northwestern.edu
Posted May 17, 2022.
Enzymatically-active bacterial microcompartments follow substrate gradients and are protected from aggregation in a cell-free system
