Purification, crystallization and preliminary crystallographic analysis of Kar9p from

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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°.

Document Type: Research Article

DOI: http://dx.doi.org/10.1107/S1744309112036342

Affiliations: Institute of Structural Biology, Helmholtz Zentrum München, German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany

Publication date: October 1, 2012

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