PMID:14993693
| Citation |
Daniels, BV, Jiang, JS and Fu, D (2004) Crystallization and preliminary crystallographic analysis of the Escherichia coli water channel AqpZ. Acta Crystallogr. D Biol. Crystallogr. 60:561-3 |
|---|---|
| Abstract |
AqpZ is a 24 kDa integral membrane protein that facilitates water movement across the plasma membrane of Escherichia coli. In this study, the first crystallization and preliminary X-ray analysis of AqpZ are described. AqpZ was overexpressed and purified with a yield of 13 mg of purified AqpZ per litre of cell culture. The purified AqpZ was shown to be a monodisperse species consisting of tetrameric protein-detergent complexes. A crystallization condition for producing diffraction-quality crystals was identified. Initial X-ray analysis indicated that the diffraction limit of AqpZ extended to 3.6 A. Crystals were found to belong to space groups P4(1)22 or P4(3)22, with unit-cell parameters a = b = 119.04, c = 380.23 A. |
| Links |
PubMed Online version:10.1107/S090744490302972X |
| Keywords |
Aquaporins/chemistry; Aquaporins/genetics; Aquaporins/metabolism; Crystallization; Crystallography, X-Ray; Detergents/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Membrane Proteins/chemistry; Membrane Proteins/genetics; Membrane Proteins/metabolism; Recombinant Fusion Proteins/chemistry; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; Water/metabolism |
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