I should have been more clear. If your protein is insoluble aggregate, you can use crystal screen results to get an idea of what buffer conditions favor solubility (and hopefully monodispersity). An example is described nicely in Collins et al, Acta Cryst F 61:1035.
Ho Ho Leung Ng University of Hawaii at Manoa Assistant Professor, Department of Chemistry h...@hawaii.edu On Wed, Feb 22, 2012 at 5:54 PM, Bernhard Rupp (Hofkristallrat a.D.) <hofkristall...@gmail.com> wrote: >> You might get lucky by setting up crystallization plates, but chances are > you won't get very useful information from them, especially if your > aggregated protein is soluble. > > I seem to fail to understand how crystallization plates would give > information in the not-special case of protein aggregates NOT being soluble? > > > BR > > Ho > > Ho Leung Ng > University of Hawaii at Manoa > Assistant Professor, Department of Chemistry h...@hawaii.edu >
