Reference: Julien S, et al. (2015) Crystallographic studies of the structured core domain of Knr4 from Saccharomyces cerevisiae. Acta Crystallogr F Struct Biol Commun 71(Pt 9):1120-4

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Abstract


The potentially structured core domain of the intrinsically disordered protein Knr4 from Saccharomyces cerevisiae, comprising residues 80-340, was expressed in Escherichia coli and crystallized using the hanging-drop vapour-diffusion method. Selenomethionine-containing (SeMet) protein was also purified and crystallized. Crystals of both proteins belonged to space group P6522, with unit-cell parameters a = b = 112.44, c = 265.21 Å for the native protein and a = b = 112.49, c = 262.21 Å for the SeMet protein, and diffracted to 3.50 and 3.60 Å resolution, respectively. There are two molecules in the asymmetric unit related by a twofold axis. The anomalous signal of selenium was recorded and yielded an electron-density map of sufficient quality to allow the identification of secondary-structure elements.

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Journal Article | Research Support, Non-U.S. Gov't
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Julien S, Tondl P, Durand F, Dagkessamanskaia A, van Tilbeurgh H, François JM, Mourey L, Zerbib D, Martin-Yken H, Maveyraud L
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