Beschreibung:
<jats:p>The potentially structured core domain of the intrinsically disordered protein Knr4 from<jats:italic>Saccharomyces cerevisiae</jats:italic>, comprising residues 80–340, was expressed in<jats:italic>Escherichia coli</jats:italic>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<jats:italic>P</jats:italic>6<jats:sub>5</jats:sub>22, with unit-cell parameters<jats:italic>a</jats:italic>=<jats:italic>b</jats:italic>= 112.44,<jats:italic>c</jats:italic>= 265.21 Å for the native protein and<jats:italic>a</jats:italic> = <jats:italic>b</jats:italic> = 112.49,<jats:italic>c</jats:italic>= 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.</jats:p>