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
>
>
> --
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> Meindert H. Lamers
> Medical Research Council
> Laboratory of Molecular Biology
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> Cambridge, CB2 0QH
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