: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).
:
