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. 2006 Sep 25;174(7):931–937. doi: 10.1083/jcb.200605179

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Copyright © 2006, The Rockefeller University Press

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Figure 2. — Hydrodynamic properties of wild-type OSM-3 and H2 mutants measured by sucrose gradient sedimentation. (a) Fractions from sucrose gradients (0 M NaCl) analyzed by SDS-PAGE. Note the shift in the sedimentation peak of OSM-3–G444E compared with wild-type OSM-3. Albumin, catalase, and ovalbumin were added as hydrodynamic standards. (b) Normalized SDS-PAGE band intensities are plotted versus fraction number for OSM-3, OSM-3–ΔH2, and OSM-3–G444E at 0 M NaCl and for wild-type (WT) OSM-3 at 1 M NaCl. (c) Table summarizing the S_20,w values measured for the three constructs at low (0 and 0.05 M) or high (0.5 and 1 M) NaCl. Values represent the mean ± SD for six to seven independent experiments for low salt. The high-salt values are from four experiments with wild type and from a single experiment with the mutants. Values from individual sucrose gradients are reported in Table S1 (available at http://www.jcb.org/cgi/content/full/jcb.200605179/DC1).