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  The structure of the aquaporin-1 water channel: A comparison between cryo-electron microscopy and X-ray crystallography

de Groot, B. L., Engel, A., & Grubmueller, H. (2003). The structure of the aquaporin-1 water channel: A comparison between cryo-electron microscopy and X-ray crystallography. Journal of Molecular Biology, 325(3), 485-493. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WK7-47G321T-9-1&_cdi=6899&_user=38661&_pii=S0022283602012330&_orig=search&_coverDate=01%2F17%2F2003&_sk=996749996&view=c&wchp=dGLzVlb-zSkzV&md5=7825b2f258095791862797b6e9195ee7&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F192-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E419-0
Genre: Journal Article

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 Creators:
de Groot, B. L.1, Author              
Engel, A., Author
Grubmueller, H.1, Author              
Affiliations:
1Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578630              

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Free keywords: cryo-electron microscopy; X-ray crystallography; structure refinement; water channel; GlpF
 Abstract: Three different medium-resolution structures of the human water channel aquaporin-1 (AQP1) have been solved by cryo-electron microscopy (cryo-EM) during the last two years. Recently, the structure of the strongly related bovine AQP1 was solved by X- ray crystallography at higher resolution, allowing a validation of the original medium-resolution structures, and providing a good indication for the strengths and limitations of state of the art cryo-EM methods. We present a detailed comparison between the different models, which shows that overall, the structures are highly similar, deviating less than 2.5 Angstrom from each other in the helical backbone regions. The two original cryo-EM structures, however, also show a number of significant deviations from the X-ray structure, both in the backbone positions of the transmembrane helices and in the location of the amino acid side-chains facing the pore. In contrast, the third cryo-EM structure that included information from the X-ray structure of the homologous bacterial glycerol facilitator GIpF and that was subsequently refined against cryo-EM AQP1 data, shows a root mean square deviation of 0.9 Angstrom from the X-ray structure in the helical backbone regions. (C) 2003 Elsevier Science Ltd. All rights reserved.

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Language(s): eng - English
 Dates: 2003-01-17
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Molecular Biology
Source Genre: Journal
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Pages: - Volume / Issue: 325 (3) Sequence Number: - Start / End Page: 485 - 493 Identifier: -