@article {10.7554/eLife.48215,
	title = {The structure of the yeast Ctf3 complex},
	journal = {eLife},
	volume = {8},
	year = {2019},
	month = {jun},
	pages = {e48215},
	publisher = {eLife Sciences Publications, Ltd},
	abstract = {Kinetochores are the chromosomal attachment points for spindle microtubules. They are also signaling hubs that control major cell cycle transitions and coordinate chromosome folding. Most well-studied eukaryotes rely on a conserved set of factors, which are divided among two loosely-defined groups, for these functions. Outer kinetochore proteins contact microtubules or regulate this contact directly. Inner kinetochore proteins designate the kinetochore assembly site by recognizing a specialized nucleosome containing the H3 variant Cse4/CENP-A. We previously determined the structure, resolved by cryo-electron microscopy (cryo-EM), of the yeast Ctf19 complex (Ctf19c, homologous to the vertebrate CCAN), providing a high-resolution view of inner kinetochore architecture (Hinshaw and Harrison, 2019). We now extend these observations by reporting a near-atomic model of the Ctf3 complex, the outermost Ctf19c sub-assembly seen in our original cryo-EM density. The model is sufficiently well-determined by the new data to enable molecular interpretation of Ctf3 recruitment and function.},
	issn = {2050-084X},
	doi = {10.7554/eLife.48215},
	url = {https://doi.org/10.7554/eLife.48215},
	author = {Hinshaw, Stephen M and Dates, Andrew N and Harrison, Stephen C},
	editor = {Musacchio, Andrea}
}
