@article{Ferguson1998inter-6877,
  year={1998},
  doi={10.1002/pro.5560070719},
  title={An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12},
  number={7},
  volume={7},
  issn={0961-8368},
  journal={Protein Science},
  pages={1636--1638},
  author={Ferguson, Andrew D. and Breed, Jason and Diederichs, Kay and Welte, Wolfram and Coulton, James W.}
}

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    <dc:creator>Ferguson, Andrew D.</dc:creator>
    <dcterms:title>An internal affinity-tag for purification and crystallization of the siderophore receptor FhuA, integral outer membrane protein from Escherichia coli K-12</dcterms:title>
    <dc:contributor>Breed, Jason</dc:contributor>
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    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:29:51Z</dc:date>
    <dcterms:bibliographicCitation>First publ. in: Protein Science 7 (1998), pp. 1636-1638</dcterms:bibliographicCitation>
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    <dc:creator>Diederichs, Kay</dc:creator>
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    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:contributor>Ferguson, Andrew D.</dc:contributor>
    <dc:creator>Coulton, James W.</dc:creator>
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    <dcterms:issued>1998</dcterms:issued>
    <dc:creator>Welte, Wolfram</dc:creator>
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    <dcterms:abstract xml:lang="eng">FhuA (M, 78,992, 714 amino acids), siderophore receptor for ferrichrome-iron in the outer membrane of Escherichia coli, was affinity tagged, rapidly purified, and crystallized. To obtain FhuA in quanties sufficient for crystallization, a hexahistidine tag was genetically inserted into the fhuA gene after amino acid 405, which resides in a known surface-exposed loop. Recombinant FhuA405.H6 was overexpressed in an E. coli strain that is devoid of several major porins and using metal-chelate chromatography was purified in large amounts to homogeneity. FhuA crystals were grown using the hanging drop vapor diffusion technique and were suitable for X-ray diffraction analysis. On a rotating anode X-ray source, diffraction was observed to 3.0 Å resolution. The crystals belong to space group P61 or P65 with unit cell dimensions of a = b = 174 Å, c = 88 Å (α = β = 90°, γ = 120").</dcterms:abstract>
    <dc:contributor>Coulton, James W.</dc:contributor>
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    <dc:contributor>Diederichs, Kay</dc:contributor>
    <dc:contributor>Welte, Wolfram</dc:contributor>
    <dc:creator>Breed, Jason</dc:creator>
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