Dear all, We recently solved a the structure of a small c-type cytochrome. We observed, that of the eleven chains in the asymmetric unit ten form 3D domain swapped dimers by exchanging an α-helix. The eleventh chain is present as a monomer. Based on the anomalous iron signal and the chain tracing we are sure that no chain was missed. I tried to find other examples in the PDB, were one crystal is made of different homo- or heterooligomers. I only found proteins with partial occupied peptide binding sites, which is not what I am looking for. Does anyone know of a case were the presence of different homo- or heterooligomers is required to form the crystal?
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