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Figure 3
Characterization of the basal and MT-stimulated ATPase activities of Kif1519–375 and Kif151–375. (a) Influence of the NaCl concentration on the basal ATPase activity of Kif1519–375 (red) and Kif151–375 (blue) in the presence of 1 mM ATP. (b) Optimization of the basal ATPase activity in the presence of increasing ATP concentrations measured at 75 mM NaCl for Kif1519–375 (red) and 50 mM NaCl for Kif151–375 (blue). (c) Salt dependence of the MT-stimulated Kif1519–375 ATPase activity (red) in the absence (circles) and in the presence of 50 mM (filled circles), 100 mM (squares) and 150 mM (filled squares) KCl and salt dependence of the MT-stimulated Kif151–375 ATPase activity (blue) in the absence (filled diamonds) and the presence (squares) of 50 mM KCl. Data were measured at increasing MT concentrations ranging from 0 to 10 µM in the presence of 1 mM ATP. (d) Optimization of the ATP concentration for the MT-stimulated ATPase activity of Kif1519–375 (red) and Kif151–375 (blue) in the presence of increasing ATP concentrations, measured at 3 µM MTs, in the absence of salt.

Journal logoBIOLOGICAL
CRYSTALLOGRAPHY
ISSN: 1399-0047
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