Hi,
I am trying to purify a recombinant protein fused to GST overproduced in
E.coli. I have some problems during the purification steps, and I
hypothesised that homodimers formation mediated by the GST moiety could
be the cause of the problem.
Does anybody know what conditions could be used to minimize the
formation of such dimers ?
I already know that there are 4 cysteines in the gst monomer and I know
that they are not involved in dimer formation, since mutation to serines
still allows dimer formation (these are results published by other
groups). I also know that in 2 M urea, the dimers are still allowed
(this is my own experience).
Thanks a lot for any suggestions
Alexandre Blais
Graduate Student
Centre de Recherche du CHUL
Québec, Canada
