Crystallographic studies of the structured core domain of Knr4 from Saccharomyces cerevisiae. Issue 9 (1st September 2015)

• Record Type: Journal Article
• Authors: Julien, Sylviane; Tondl, Patrick; Durand, Fabien; Dagkessamanskaia, Adilia; van Tilbeurgh, Herman; François, Jean Marie; Mourey, Lionel; Zerbib, Didier; Martin‐Yken, Hélène; Maveyraud, Laurent
• Is Part Of: Acta crystallographica. Volume 71:Issue 9(2015:Sep.)
• Page Start: 1120
• Page End: 1124
• Publication Date: 2015-09-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X15012522
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The potentially structured core domain of the intrinsically disordered protein Knr4 from <italic>Saccharomyces cerevisiae</italic>, comprising residues 80–340, was expressed in <italic>Escherichia coli</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 <italic>P</italic>6₅22, with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 112.44, <italic>c</italic> = 265.21 Å for the native protein and <italic>a</italic> = <italic>b</italic> = 112.49, <italic>c</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.</p> </abstract>