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Effect of increasing monovalent-cation concentration on the poly(U)-stimulated ATPase activity of MBP-nsp10. The ATPase activity was analyzed by thin-layer chromatography using [γ-32P]ATP as a substrate as described in Materials and Methods and quantified by phosphorimaging. The poly(U)-stimulated ATPase activity in the absence of potassium chloride was taken to be 100%, and all other activities were normalized to this value (see text for details).
