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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Aquaporins / chemistry*
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Aquaporins / genetics
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Aquaporins / metabolism
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Crystallization
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Crystallography, X-Ray
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Detergents / chemistry
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism
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Membrane Proteins / chemistry*
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Membrane Proteins / genetics
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Membrane Proteins / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Water / metabolism
Substances
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Aquaporins
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Detergents
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Escherichia coli Proteins
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Membrane Proteins
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Recombinant Fusion Proteins
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aqpZ protein, E coli
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Water