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Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism.

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Aponte-Santamaria,  C. A.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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de Groot,  B. L.
Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Fischer, G., Kosinska-Eriksson, U., Aponte-Santamaria, C. A., Palmgren, M., Geijer, M., Hedfalk, K., et al. (2009). Crystal structure of a yeast aquaporin at 1.15 angstrom reveals a novel gating mechanism. PLoS Biology, 7(6): e1000130. doi:10.1371/journal.pbio.1000130.


Cite as: https://hdl.handle.net/11858/00-001M-0000-000F-9C03-0
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