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Title: Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 Å
Authors: Torres, Jaume
Ruiz Carrillo, David
To Yiu Ying, Janet
Darwis, Dina
Soon, Cin Huang
Cornvik, Tobias
Lescar, Julien
Keywords: DRNTU::Science::Biological sciences::Microbiology::Bacteria
Issue Date: 2014
Source: Ruiz Carrillo, D., To Yiu Ying, J., Darwis, D., Soon, C. H., Cornvik, T., Torres, J., et al. (2014). Crystallization and preliminary crystallographic analysis of human aquaporin 1 at a resolution of 3.28 Å. Acta crystallographica section F : structural biology communications, 70(12), 1657-1663.
Series/Report no.: Acta crystallographica section F : structural biology communications
Abstract: Aquaporin water channels (AQPs) are found in almost every organism from humans to bacteria. In humans, 13 classes of AQPs control water and glycerol homeostasis. Knockout studies have suggested that modulating the activity of AQPs could be beneficial for the treatment of several pathologies. In particular, aquaporin 1 is a key factor in cell migration and angiogenesis, and constitutes a possible target for anticancer compounds and also for the treatment of glaucoma. Here, a preliminary crystallographic analysis at 3.28 Å resolution of crystals of human aquaporin 1 (hAQP1) obtained from protein expressed in Sf9 insect cells is reported. The crystals belonged to the tetragonal space group I422, with unit-cell parameters a = b = 89.28, c = 174.9 Å, and contained one monomer per asymmetric unit. The hAQP1 biological tetramer is generated via the crystallographic fourfold axis. This work extends previous electron crystallo­graphic studies that used material extracted from human red blood cells, in which the resolution was limited to approximately 3.8 Å. It will inform efforts to improve lattice contacts and the diffraction limit for the future structure-based discovery of specific hAQP1 inhibitors.
ISSN: 2053-230X
DOI: 10.1107/S2053230X14024558
Schools: School of Biological Sciences 
Rights: © 2014 International Union of Crystallography. This paper was published in Acta Crystallographica Section F: Structural Biology Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [].  One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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