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Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form.

ABSTRACT: Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 A resolution despite a high degree of merohedral twinning. This is the first report of crystallographic data on 'as-isolated' E. coli bacterioferritin. The ferroxidase active site contains positive difference density consistent with two metal ions that had co-purified with the protein. X-ray fluorescence studies suggest that the metal composition is different from that of previous structures and is a mix of zinc and native iron ions. The ferroxidase-centre configuration displays a similar flexibility as previously noted for other bacterioferritins.

SUBMITTER: van Eerde A

PROVIDER: S-EPMC2225212 | biostudies-literature | 2006 Nov

REPOSITORIES: biostudies-literature

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Fortuitous structure determination of 'as-isolated' Escherichia coli bacterioferritin in a novel crystal form.

van Eerde André A Wolterink-van Loo Suzanne S van der Oost John J Dijkstra Bauke W BW

Acta crystallographica. Section F, Structural biology and crystallization communications 20061025 Pt 11

Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 A resolution despite a high degree of merohedral twinning. This is the first report of crystallographic data on 'as-isolated' E. coli bacterioferritin. The ferroxidase active site contains positive difference density consistent with two metal ions that had co-purified with the protein. X-ray fluorescence studies suggest that the metal composition is differ ...[more]

PMID: 17077480

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