Location of haem in bacterioferritin of E. coli
. A low‐resolution partial structure of bacterioferritin was solved using a combination of molecular replacement and rigid‐body refinement methods. Modification of bacterioferritin crystals by soaking in tetrachloroplatinate results in a phase transition from tetragonal symmetry (space group P42212)...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1993-11, Vol.49 (6), p.597-600 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | . A low‐resolution partial structure of bacterioferritin was solved using a combination of molecular replacement and rigid‐body refinement methods. Modification of bacterioferritin crystals by soaking in tetrachloroplatinate results in a phase transition from tetragonal symmetry (space group P42212) to a pseudo‐cubic one (approximate space group I432). Helical parts of human H ferritin structure stripped of side chains beyond the Cβ atoms were used as the model. An electron‐density map of the refined model revealed a region of extended density which by its shape and position in a pocket between helices was identified as haem. Inclusion of haem in the refinement showed that it can occupy only one of two symmetry‐related sites near a twofold axis of the molecule. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444993007073 |