Hi Rain, try both is my advice. In some cases we (www.sgpp.org) were unsuccessful in soaking but successful in co-crystallization. I assume your question is directed towards ligands. If you are in the comfortable situation of having your own structure at hand, check out a) crystal lattice contacts - would they hamper soaking by restricting access to your site ? b) do you want to exchange an existing ligand/co-factor in your protein, then it's probably more likely to occur in solution c) how's your ligand behaving under your crystallization condition, if it crashes out try to form a complex in solution and then co-crystallize. Another tip, use your apo-form crystals to streak seed crystallization attempts with new ligands. When you co-crystallize play with the molarity ratio of your ligand.
Jürgen Bosch et al. Using fragment cocktail crystallography to assist inhibitor design of Trypanosoma brucei nucleoside 2-deoxyribosyltransferase. J Med Chem (2006) vol. 49 (20) pp. 5939-46 @Eric, can you comment on this: Ojo et al. Toxoplasma gondii calcium-dependent protein kinase 1 is a target for selective kinase inhibitors. Nat Struct Mol Biol (2010) vol. 17 (5) pp. 602-7 On May 15, 2010, at 7:47 AM, rainfieldcn wrote: > Hi, friends: > Is there any published paper describing the case study of the difference > between co-crystallization and crystal soaking? > I mean has anybody observed different structures by these two methods? > Thank you! > > Rain Fieldcn > 2010-05-15 - Jürgen Bosch Johns Hopkins Bloomberg School of Public Health Department of Biochemistry & Molecular Biology Johns Hopkins Malaria Research Institute 615 North Wolfe Street, W8708 Baltimore, MD 21205 Phone: +1-410-614-4742 Lab: +1-410-614-4894 Fax: +1-410-955-3655 http://web.mac.com/bosch_lab/
