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

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.

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Fischer, G., Author
Kosinska-Eriksson, U., Author
Aponte-Santamaria, C. A.1, Author              
Palmgren, M., Author
Geijer, M., Author
Hedfalk, K., Author
Hohmann, S., Author
de Groot, B. L.1, Author              
Neutze, R., Author
Lindkvist-Petersson, K., Author
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, 578573              

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Language(s): eng - English
 Dates: 2009
 Publication Status: Published online
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 Rev. Type: Peer
 Identifiers: DOI: 10.1371/journal.pbio.1000130
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Title: PLoS Biology
Source Genre: Journal
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Pages: 13 Volume / Issue: 7 (6) Sequence Number: e1000130 Start / End Page: - Identifier: -