Afshan

Radaev and Sun published a paper a few years ago showing that
crystallization conditions for complexes are strongly biased towards PEG
conditions (rather than e.g. high salt conditions).  The reference is below.

I would use microseeding into random screens [2], using the crystals that
you have as seed crystals.  Ideally you should find conditions where *both
the complex and the seed stock are stable*.  By coincidence we had a paper
accepted this week by Crystal Growth and Design on this exact topic, see
below.

Best wishes

Patrick

______________________

[1] Radaev, S; Sun, P.D. J. Appl. Crystallogr. 2002, 35, 674-676.

[2] D'Arcy, A.; Villard, F.; Marsh, M. Acta Crystallogr. 2007, D63, 550-554.

[3] Patrick D. Shaw Stewart , Stefan A. Kolek , Richard A. Briggs , Naomi E.
Chayen , and Peter Baldock
Cryst. Growth Des., Just Accepted Manuscript.  "Random microseeding: a
theoretical and practical exploration of seed stability and seeding
techniques for successful protein crystallization".
http://pubs.acs.org/doi/abs/10.1021/cg2001442




On Fri, May 27, 2011 at 1:24 PM, Afshan Begum <[email protected]> wrote:

> Dear All,
>
> I have a severe prob lam to performed my ligand binding study with
> corresponding protein. I have taking the native diffraction data at 1.75 A
> and after that i have performed soaking as well co-crystallization
> experiment with my inhibitors.
> Problem is that at the active site phosphate ion always bind instead of
> inhibitors. I have  used 1.6 M ammonium phosphate conc at the
> crystallization recipe which is a very weak inhibitor of my protein whereas
> the ligand is already clinically applicable but due to the very high conc.
> of phosphate i have not achieved my target. If some one can suggest me what
> else i can replace with ammonium phosphate or any other suggestions would be
> appreciated.
>
> I have tried to grown crystals some other condition but the crystal was not
> diffracted beyond 3.5 A.
>
> Best Regards
>
> AFSHAN
>



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