Stable kinetochore-microtubule attachments are essential for cell division. It requires recruitment of outer kinetochore microtubule binders by centromere proteins C and T (CENP-C and CENP-T). We reconstituted the binding of the MIS12 and NDC80 outer kinetochore subcomplexes to CENP-C and CENP-T. Whereas CENP-C recruits a single MIS12:NDC80 complex, CENP-T simultaneously binds one MIS12:NDC80 and two NDC80 complexes upon phosphorylation at three distinct CENP-T sites. Visualization of reconstituted complexes by electron microscopy highlights how outer kinetochore modules bridge distances of well over 100 nm. This work was recently made available here: http://www.biorxiv.org/content/early/2016/08/25/071613. I will discuss the importance of the observed NDC80 multivalency on kinetochore-microtubule interactions and describe how reconstituted kinetochores hold the potential to probe with unprecedented control how this large macromolecular machine operates.