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. 1998 Nov 2;143(3):673–685. doi: 10.1083/jcb.143.3.673

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Dimerization of the Xklp2-Tail. (A) Silver-stained SDS-PAGE of thrombin-cleaved Xklp2-Tail incubated with increasing amounts of glutaraldehyde (from left to right: markers, 0, 0.0003, 0.001, 0.003, and 0.01%). With rising glutaraldehyde concentrations, a new band appears at 60 kD corresponding to the dimeric Xklp2-Tail. The molecular mass of marker proteins is indicated on the left. (B) Far UV circular dichroism spectra of Xklp2-Tail (solid line), CDel2 (long dash), and NDel2 (short dash) at 2 μM concentration at 4°C. (C) Thermal unfolding of Xklp2-Tail (filled circle), CDel2 (open circle), NDel1 (triangle), NDel2 (upsidedown triangle) at 10 μM. (D) Thermal unfolding of Xklp2-NDel2 at a concentration of 10 μM (filled circle) and 1 μM (open circle). (E) Thermal unfolding of GST-Xklp2-Tail (filled circle) and Xklp2-Tail (open circle) at 10 μM concentration. See text for details.