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Protein Science, Vol 7, Issue 7 1636-1638, Copyright © 1998 by Cold Spring Harbor Laboratory Press
FOR THE RECORD |
A. D. FERGUSON, J. BREED, K. DIEDERICHS, W. WELTE and J. W. COULTON
Department of Microbiology and Immunology, McGill University, 3775 University Street, Montreal, Quebec, Canada H3A 2B4 Fakultat fur Biologie, Universitat Konstanz, Universitatsstrasse 10, Postfach 5560 (M656), D-78457 Konstanz, Germany
FhuA (M(r) 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.H(6) 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{deg}, {gamma} = 120{deg}).
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