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Crystallographic studies of the structured core domain of Knr4 from Saccharomyces cerevisiae

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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Submitted on : Friday, September 28, 2018 - 10:18:47 AM
Last modification on : Tuesday, January 5, 2021 - 3:00:06 PM

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Sylviane Julien, Patrick Tondl, Fabien Durand, Adilia Dagkessamanskaia, Herman van Tilbeurgh, et al.. Crystallographic studies of the structured core domain of Knr4 from Saccharomyces cerevisiae. Acta crystallographica. Section F, Structural biology communications, John Wiley & Sons Ltd,, 2015, 71 (9), pp.1120 - 1124. ⟨10.1107/S2053230X15012522⟩. ⟨hal-01883404⟩

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