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• W2124274290 abstract "FhuA (Mr 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 quantities 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 A resolution. The crystals belong to space group P6(1) or P6(5) with unit cell dimensions of a=b=174 A, c=88 A (alpha=beta=90 degrees, gamma=120 degrees)." @default.
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• W2124274290 date "1998-07-01" @default.
• W2124274290 modified "2023-10-14" @default.
• W2124274290 title "An internal affinity-tag for purification and crystallization of the siderophore receptor fhua, integral outer membrane protein from<i>escherichia coli</i>K-12" @default.
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• W2124274290 doi "https://doi.org/10.1002/pro.5560070719" @default.
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