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Ribosomal proteins in most procaryotic and eucaryotic cells are basic in ionic character. Notable exceptions are the acidic ribosomal proteins from the extreme halophilic bacterium, Halobacterium cutirubrum. The identification of the protein moieties involved in these and other interactions in the halophile ribosome requires a rapid and reproducible screening method for the separation, enumeration and identification of these acidic polypeptides in the complex ribosomal protein mixtures. In this paper the authors present the results of analyses of the halophile ribosomal proteins using a two-dimensional polyacrylamide gel electrophoresis system. This system separates the proteins of the 30 S and 50 S ribosomal subunis of H. cutirubrum, ascribes 21 proteins to the 30 S and 32 to the 50 S subunit and yields values for the molecular weight.