Dear Pascal,
be aware that fos-choline detergents are extremely efficient solubilizers of
membrane proteins. We found that even partially aggregated membrane proteins
could be solubilized with fos-choline 12, while this fraction did sediment
using for example dodecylmaltoside (see e.g. fig5 and
Hi Pascal,
I suspect the protein is aggregating in the presence of
FosCholine. In addition to the suggestions made by others, you can
also try changing the salt concentration or including additives like
glycerol in your FosCholine buffer. This can make an enormous
difference in the stability
A crude purification prior loading the metal-chelating column (like ion
exchange chromatography) can help and speed up the binding to the column
(remark not specific to Fos-cholin). Fos-choline is, contrary to
popular belief, a quite harsh detergent and this may affect the
purification yield a
Dear Pascal,
There can be a number of reasons for this. Maybe fos-cholines are not very well
suited for your membrane proteins of interest? - have you checked for activity
or aggregation and compared to other detergents? If the detergent is optimal
you may consider moving/extending the tag or c
Dear All,
I apologize for the not strictly crystallography-related query.
I am currently purifying several membrane proteins solubilized in
fos-cholines detergents and I consistently observe a significant loss of
protein at the binding step (done in absence of imidazole). Has anyone else
experienc
