| People | Locations | Statistics |
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| Naji, M. |
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| Motta, Antonella |
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| Aletan, Dirar |
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| Mohamed, Tarek |
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| Ertürk, Emre |
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| Taccardi, Nicola |
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| Kononenko, Denys |
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| Petrov, R. H. | Madrid |
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| Alshaaer, Mazen | Brussels |
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| Bih, L. |
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| Casati, R. |
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| Muller, Hermance |
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| Kočí, Jan | Prague |
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| Šuljagić, Marija |
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| Kalteremidou, Kalliopi-Artemi | Brussels |
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| Azam, Siraj |
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| Ospanova, Alyiya |
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| Blanpain, Bart |
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| Ali, M. A. |
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| Popa, V. |
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| Rančić, M. |
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| Ollier, Nadège |
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| Azevedo, Nuno Monteiro |
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| Landes, Michael |
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| Rignanese, Gian-Marco |
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Spiliopoulou, Maria
University of Patras
in Cooperation with on an Cooperation-Score of 37%
Topics
Publications (7/7 displayed)
- 2021High-throughput macromolecular polymorph screening via an NMR and X-ray powder diffraction synergistic approach: the case of human insulin co-crystallized with resorcinol derivativescitations
- 2020Insulin polymorphism induced by two polyphenols: new crystal forms and advances in macromolecular powder diffractioncitations
- 2019Unit-cell response of tetragonal hen egg white lysozyme upon controlled relative humidity variationcitations
- 2019Revisiting the structure of a synthetic somatostatin analogue for peptide drug designcitations
- 2018<i>In situ</i>detection of a novel lysozyme monoclinic crystal form upon controlled relative humidity variationcitations
- 2017Dengue virus 3 NS5 methyltransferase domain: expression, purification, crystallization and first structural data from microcrystalline specimenscitations
- 2016Coxsackievirus B3 protease 3C: expression, purification, crystallization and preliminary structural insightscitations
Places of action
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article
Coxsackievirus B3 protease 3C: expression, purification, crystallization and preliminary structural insights
Abstract
<jats:p>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%(<jats:italic>w</jats:italic>/<jats:italic>v</jats:italic>) PEG 4000, 0.1 <jats:italic>M</jats:italic>Tris–HCl, 0.2 <jats:italic>M</jats:italic>MgCl<jats:sub>2</jats:sub>in a pH range from 7.0 to 8.5. A polymorph of monoclinic symmetry (space group<jats:italic>C</jats:italic>2, unit-cell parameters<jats:italic>a</jats:italic> = 77.9,<jats:italic>b</jats:italic>= 65.7,<jats:italic>c</jats:italic> = 40.6 Å, β = 115.9°) was identified<jats:italic>via</jats:italic>XRPD. These results are the first step towards the complete structural determination of the molecule<jats:italic>via</jats:italic>XRPD and a parallel demonstration of the accuracy of the method.</jats:p>