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Crystallographic studies of the structured core domain of Knr4 from Saccharomyces cerevisiae
Author(s) -
Julien Sylviane,
Tondl Patrick,
Durand Fabien,
Dagkessamanskaia Adilia,
van Tilbeurgh Herman,
François Jean Marie,
Mourey Lionel,
Zerbib Didier,
MartinYken Hélène,
Maveyraud Laurent
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15012522
Subject(s) - saccharomyces cerevisiae , crystallography , chemistry , resolution (logic) , selenium , domain (mathematical analysis) , diffraction , escherichia coli , yeast , biochemistry , physics , mathematics , organic chemistry , computer science , optics , mathematical analysis , artificial intelligence , gene
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 P 6 5 22, 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.