In article <Pine.SOL.4.33.0301131030090.19612-100000 at mcmail.cis.mcmaster.ca>, Kyle Legate <legatek at mcmail.cis.mcmaster.ca> wrote:
>On 13 Jan 2003 mrsankar_in at yahoo.co.uk wrote:
>>> I have a His Tag protein overexpressed in E.coli and it does not go into
> inclusion bodies. I want to crystallize the protein for which i need it in a
> very high concentration and in very pure form. What way i can purify the
> protein in Ni Column? Denaturing or native conditions?
This is all protein-dependent. Try and see what works best for your
protein.
>What info do you hope to gain from a crystal of denatured protein?
If a protein is partially folded/denatured, it can give a nice idea
about folding pathway(s). Problem is, such things seem to never
crystallize. I know I tried :-)
But I think the original poster simply wants to purify a [folded]
protein and does not know how to proceed.
DK
