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• W2016993713 abstract "IRS-2 from the hard tick Ixodes ricinus belongs to the serpin family of protease inhibitors. It is produced in the salivary glands of the tick and its anti-inflammatory activity suggests that it plays a role in parasite–host interaction. Recombinant IRS-2 prepared by heterologous expression in a bacterial system was crystallized using the hanging-drop vapour-diffusion method. The crystals belonged to the primitive tetragonal space group P43 and diffracted to 1.8 Å resolution. Mass-spectrometric and electrophoretic analyses revealed that IRS-2 was cleaved by contaminating proteases during crystallization. This processing of IRS-2 mimicked the specific cleavage of the serpin by its target protease and resulted in a more stable form (the so-called relaxed conformation), which produced well diffracting crystals. Activity profiling with specific substrates and inhibitors demonstrated traces of serine and cysteine proteases in the protein stock solution." @default.
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• W2016993713 date "2010-10-28" @default.
• W2016993713 modified "2023-10-18" @default.
• W2016993713 title "Crystallization and diffraction analysis of the serpin IRS-2 from the hard tick<i>Ixodes ricinus</i>" @default.
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• W2016993713 doi "https://doi.org/10.1107/s1744309110032343" @default.
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