Julien Sylviane, Tondl Patrick, Durand Fabien, Dagkessamanskaia Adilia, van Tilbeurgh Herman, François Jean Marie, Mourey Lionel, Zerbib Didier, Martin-Yken Hélène, Maveyraud Laurent
Institut de Pharmacologie et de Biologie Structurale (IPBS), Centre National de la Recherche Scientifique (CNRS), 205 Route de Narbonne, BP 64182, 31077 Toulouse, France.
Université de Toulouse, INSA, UPS, INP, LISBP, 135 Avenue de Rangueil, 31077 Toulouse, France.
Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1120-4. doi: 10.1107/S2053230X15012522. Epub 2015 Aug 25.
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.
酿酒酵母中内在无序蛋白Knr4的潜在结构化核心结构域（包含第80至340位残基）在大肠杆菌中表达，并采用悬滴气相扩散法进行结晶。还纯化并结晶了含硒代甲硫氨酸（SeMet）的蛋白。两种蛋白的晶体均属于P6522空间群，天然蛋白的晶胞参数为a = b = 112.44 Å，c = 265.21 Å，SeMet蛋白的晶胞参数为a = b = 112.49 Å，c = 262.21 Å，衍射分辨率分别为3.50 Å和3.60 Å。不对称单元中有两个通过二重轴相关的分子。记录了硒的反常信号，并生成了质量足以识别二级结构元件的电子密度图。
