Dear CCP4 community, Sorry for this off-topic protein purification problem.I'm trying to purify an immunoglobulin-like beta sheet protein with a c-terminus HIS construct. The protein expressed both in the supernat and pellet ( majority ). I purified the supernat and after run gel filtration, it's in the void volume. I also tried to purify from the pellet,and do dialysis refolding ( with and without L-arg ), after overnight dialysis, I run the gel filtration column, the apparent molecular weight looks like dimer/trimer. But when I did a CD scan of the protein, it's showing an unfolded protein profile.I was wondering if there is anyway to promote folding,or if anyway that can make some mutations to make it foldable.Any input would be useful.
Thanks a lot. Jenny
