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Figure 2
Crystal structures of B. melitensis bacterioferritin. (a) 24-subunit assembly creating a 12 nm outer diameter shell with an 8 nm interior cavity. (b) Comparison of the dimer accommodating the heme cofactor (green) in the holo BmBfr structure (left, white) or without cofactor (apo BmBfr, blue, right). An alignment of this interface in both structures is presented (middle). (c) Comparison of the ferroxidase centers in the holo BmBfr (left) or apo BmBfr structures (right). (d) Picture of apo BmBfr crystals. |

journal menu![[Figure 2]](jb5073fig2.jpg)
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