Try first to give it a shot and see if you get crystals without too much hassle and expense. I would recommend a size exclusion chromatography step after refolding and from that collect a uniform sample for crystallization.
Poul On 12/07/2010, at 13.39, meindert lamers wrote: > Dear all, > > I can get large amounts of a protein that is purified from inclusion bodies. > The protein is solubilized using 6M urea and refolded by dialysis. > > However, treatment with urea is known to modify proteins (N-term/Lys/Arg), > which could ultimately effect crystallization. > > Is this something that people generally worry about? > For example > -would you bother cleaning up the urea by ion exchange > -get ultra pure urea (ultra $$$) > -change to guanidinium chloride > -hope that it might benefit crystallization (i.e. similar to methylation of > lysines) > > > Thanks in advance, > Meindert > > > -- > ************************** > Meindert H. Lamers > Medical Research Council > Laboratory of Molecular Biology > Hills Road, > Cambridge, CB2 0QH > United Kingdom > tel +44 (0)1223 402401 > fax +44 (0)1223 213556 > web: http://www2.mrc-lmb.cam.ac.uk/groups/mlamers/ > **************************
