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. 2007 May 30;81(16):8384–8395. doi: 10.1128/JVI.00564-07

FIG. 2.

FIG. 2.

Expression and purification of EAV nsp9/RdRp-His. Coomassie brilliant blue staining of a sodium dodecyl sulfate-polyacrylamide gel showing the two-step purification of the enzyme by Ni-NTA affinity chromatography (Ni-NTA) and S200 gel filtation (GF). C, total protein in the cell lysate; FT, flowthrough; S, soluble fraction; W, waste fraction; P, peak fraction; 26, fraction 26 of the Ni-NTA eluate; M, molecular size marker. On the right side of the gel, different fractions of the run on the S200 gel filtration column are shown. Fractions 32 to 36 were pooled to obtain the nsp9/RdRp-His preparation used in this study.