Dear all, I'm searching for examples of crystal structures that show a clear asymmetry in the dimeric/oligomeric state. This asymmetry should not have been induced by the crystal packing (e.g. two domains connected by a long linker packing different, termini/loops which interact differently with the surrounding) rather than by an internal asymmetry (which may be confirmed by other techniques e.g. SAXS).
The reason I'm asking: I have solved a couple of crystal structures of a chimera protein (110 residues, dimeric, 1.2 A resolution) and mutants of the same fragment consisting of basically two four helix bundles and a short connector fragment and these are highly asymmetric (although the H-bond pattern of the helix residues doesn't change) while the same structures solved by NMR are symmetric and largely different. PISA gives a variety of contacts (H-bonds, salt bridges) between the two chains, interface seems ok, stable, low B-factors). Any comments and suggestions are appreciated Best wishes and thanks! Kornelius ---------------------------------------------- Kornelius Zeth Max Planck Institute for Developmental Biology Dept. Protein Evolution Spemannstr. 35 72076 Tuebingen, Germany [EMAIL PROTECTED] Tel -49 7071 601 323 Fax -49 7071 601 349
