Guillet Valérie, Keller Daniel, Prévost Gilles, Mourey Lionel
Groupe de Biophysique Structurale, Département 'Mécanismes Moléculaires des Infections Mycobactériennes', IPBS-CNRS, 205 Route de Narbonne, 31077 Toulouse CEDEX, France.
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):310-3. doi: 10.1107/S090744490302910X. Epub 2004 Jan 23.
Class S proteins of staphylococcal bicomponent pore-forming leucotoxins play an important role in membrane targetting and cell specificity. Wild-type and recombinant S components of the Panton-Valentine leucocidin (LukS-PV) were expressed in Staphylococcus aureus and Escherichia coli, respectively, and purified. Both proteins were crystallized in two crystal forms with Jeffamine M-600 as the precipitant at 285 K using the hanging-drop vapour-diffusion method and seeding techniques. Crystals belong to space group P2 (or P2(1)) and P4(1) (or P4(3)), with unit-cell parameters a = 72.3, b = 95.1, c = 108.1 A, beta = 106.4 degrees and a = b = 94.8, c = 306.2 A, respectively. A full set of X-ray diffraction data was collected to 2.1 A from a single tetragonal crystal of the wild-type protein at 100 K.
葡萄球菌双组分成孔白细胞毒素的S类蛋白在膜靶向和细胞特异性方面发挥着重要作用。分别在金黄色葡萄球菌和大肠杆菌中表达并纯化了潘顿-瓦伦丁杀白细胞素（LukS-PV）的野生型和重组S组分。使用悬滴气相扩散法和接种技术，以Jeffamine M-600作为沉淀剂，在285 K下将两种蛋白质结晶为两种晶体形式。晶体分别属于空间群P2（或P2(1)）和P4(1)（或P4(3)），晶胞参数分别为a = 72.3，b = 95.1，c = 108.1 Å，β = 106.4°和a = b = 94.8，c = 306.2 Å。在100 K下从野生型蛋白的单个四方晶体收集了完整的X射线衍射数据，分辨率达到2.1 Å。
