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. 2008 May 5;181(3):411–419. doi: 10.1083/jcb.200802189

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© 2008 Kim et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 2. — CENP-E is a highly flexible, dimeric kinesin with a 230-nm discontinuous coiled coil. (A) Coomassie- and silver-stained Xenopus full-length CENP-E (340 kD) purified to near homogeneity from baculovirus-induced insect cells. (B) Electron micrographs of individual CENP-E molecules. Two motor heads are clearly visible, as indicated by yellow arrows. (C) Length distribution of CENP-E. Contour lengths of molecules were measured, and the mean length of CENP-E was 230 ± 25 nm (mean ± SD; n = 20). (D) Coiled-coil prediction of Xenopus CENP-E. Coiled-coil scores were generated using Protean software (DNAstar) and are graphed below the amino acid scale bar. The number 1.3 is the default value indicating the minimum score for known coiled coils, and resulting predicted coiled-coil domains are shown as solid orange rectangles.