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A procedure is described for the transfer of protein crystals from an ammonium sulfate-containing mother liquor to a solution with another precipitant, such as polyethylene glycol. The suitable concentration of the alternative precipitant is established via a novel protocol, using a hanging-drop equilibration method. This crystal transfer procedure is illustrated by experiments with crystals of trypanosomal triosephosphate isomerase and bacterial p-hydroxybenzoate hydroxylase, but it might have more general applicability.

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