Structure of a Monoclinic Crystal Form of Cytochrome b1 (Bacterioferritin) from E. coli

Crystals of E. coli cytochrome b1, alias bacterioferritin, were grown from a low ionic strength solution. The resulting monoclinic P21 structure was solved by molecular replacement and refined using noncrystallographic symmetries applied to the fundamental unit, consisting of two protein subunits an...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1998-01, Vol.54 (1), p.16-24
Main Authors: Dautant, Alain, Meyer, Jean-Brice, Yariv, Joseph, Précigoux, Gilles, Sweet, Robert M., Kalb (Gilboa), A. Joseph, Frolow, Felix
Format: Article
Language:English
Online Access:Get full text
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Summary:Crystals of E. coli cytochrome b1, alias bacterioferritin, were grown from a low ionic strength solution. The resulting monoclinic P21 structure was solved by molecular replacement and refined using noncrystallographic symmetries applied to the fundamental unit, consisting of two protein subunits and a single haem. From the Patterson self‐rotation results it was shown that the asymmetric unit of the monoclinic crystal consists of 12 such dimers and corresponds to a complete, nearly spherical, molecule of bacterioferritin (Mr = 450 kDa) of 432 point‐group symmetry. It is thus the most symmetrical cytochrome. As previously determined for the tetragonal form, the haem is located in a special position on a local twofold axis of the dimer. A bimetal centre is also observed within the four‐helix bundle of each monomer; a metal‐binding site is located on the fourfold axis.
ISSN:1399-0047
1399-0047
DOI:10.1107/S0907444997006811