protein dialysis - (Aug/17/2006 )

I have to dilyze my protein. I have my protein still in elution buffer which is 250mM imidazole, 300mM NaCl and 50 mM Sodium Phosphate. I am purifying through affinity chromatography.
I have some question for dialysis. First of all i do need to precipitat my protein before dialysis.
At the moment i am just looking for my protein either its stable after remoal of tags or not in buffer. after confriming it i will purify mass volume and i have juts small voulme of my preotin in elution buffer.
Second for dialysis which buffer i have to choose and i have my dialysis tube in cold roon in I mM EDTA. I do need it wash it with water and biol it in water or i can use direct from buffer.
please give me exact protocol for this.
regards

It seems as though you have been able to purify your protein in its folded state, yes? If so, what buffer do you need to use for your next step? It should simply be a matter of changing to those conditions.
If your protein is too dilute to use as is, you can concentrate it by ion exchange (which will also double as a nice "polishing" step if you require high purity), or if it's hydrophobic, by hydrophobic interaction chromatography.