Coxsackievirus B3 protease 3C: Expression, purification, crystallization and preliminary structural insights

Stavroula Fili, Alexandros Valmas, Magdalini Christopoulou, Maria Spiliopoulou, Nikos Nikolopoulos, Julie Lichière, Souzana Logotheti, Fotini Karavassili, Eleftheria Rosmaraki, Andrew Fitch, Jonathan Wright, Detlef Beckers, Thomas Degen, Gwilherm Nénert, Rolf Hilgenfeld, Nicolas Papageorgiou, Bruno Canard, Bruno Coutard, Irene Margiolaki*

*Corresponding author for this work


Viral proteases are proteolytic enzymes that orchestrate the assembly of viral components during the viral life cycle and proliferation. Here, the expression, purification, crystallization and preliminary X-ray diffraction analysis are presented of protease 3C, the main protease of an emerging enterovirus, coxsackievirus B3, that is responsible for many cases of viral myocarditis. Polycrystalline protein precipitates suitable for X-ray powder diffraction (XRPD) measurements were produced in the presence of 22-28%(w/v) PEG 4000, 0.1 M Tris-HCl, 0.2 M MgCl2 in a pH range from 7.0 to 8.5. A polymorph of monoclinic symmetry (space group C2, unit-cell parameters a = 77.9, b = 65.7, c = 40.6 Å, β = 115.9) was identified via XRPD. These results are the first step towards the complete structural determination of the molecule via XRPD and a parallel demonstration of the accuracy of the method.The expression, purification, crystallization, X-ray powder diffraction data collection and preliminary analysis of protease 3C from coxsackievirus B3 are reported.

Original languageEnglish
JournalActa Crystallographica Section:F Structural Biology Communications
Issue number12
Pages (from-to)877-884
Number of pages8
Publication statusPublished - 01.12.2016


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