Fortuitous structure determination of as-isolated Escheria coli bacterioferritin in a novel crystal form

A. van Eerde, S. Wolterink-van Loo, J. van der Oost, B. Dijkstra

Research output: Contribution to journalArticleAcademicpeer-review

20 Citations (Scopus)

Abstract

Escherichia coli bacterioferritin was serendipitously crystallized in a novel cubic crystal form and its structure could be determined to 2.5 Å 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
Original languageEnglish
Pages (from-to)1061-1066
JournalActa Crystallographica Section F. Structural Biology and Crystallization Communications
Volume62
Issue number11
DOIs
Publication statusPublished - 2006

Keywords

  • azotobacter-vinelandii
  • iron
  • proteins
  • ferritin
  • site
  • ferroxidase
  • geometry
  • insights
  • binding

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