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Kar9p is required for correct positioning of the mitotic spindle in Saccharomyces cerevisiae. The in vivo function of Kar9p is well understood, but no structural information is available. Additionally, molecular details of how Kar9p interacts with other proteins are scarce. Full-length Kar9p was expressed in Escherichia coli, purified and crystallized. Diffraction data were collected and processed at 7 Å resolution. One crystal showed diffraction to 3 Å resolution. The crystals that diffracted to 7 Å resolution belonged to space group P3, with unit-cell parameters a = b = 195.02, c = 257.15 Å, α = β = 90, γ = 120°. The crystal that diffracted to 3 Å resolution belonged to space group P222, with unit-cell parameters a = 46.37, b = 74.64, c = 133.63 Å, α = β = γ = 90°.

Supporting information

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Portable Network Graphics (PNG) image https://doi.org/10.1107/S1744309112036342/pu5379sup1.png
Supplementary Figure 1. Example of fractions of purified full-length Kar9p after size-exclusion chromatography. The protein was over 90% pure and was stable for days.


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