Dear ALL;
I am sorry for this off-topic question about analytic ultracentrifugation
(AUC).
We recently solved one structure from crystals grown out of PEG4000 plus
buffer. Since the crystal was grown from PEG, we think the protein would
maintain its native oligomerization state as in the solution.
Indeed, the crystal packing clearly shows a tetramer of this protein.
However, both the gel-filtration and AUC showed larger molecular weight,
roughly around 6-mer or 7-mer.
IN the crystal lattice, we could not find any 6-mer or 7-mer state.
Could anyone give some comments on this discrepancy?
Thanks a lot and have a nice weekend!
Jerry McCully
