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

Acta Crystallographica. Section F, Structural Biology Communications
Sylviane JulienLaurent Maveyraud

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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Citations

May 21, 2016·Cellular Microbiology·Hélène Martin-YkenDidier Zerbib

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