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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
Dengue virus 3 NS5 methyltransferase domain: expression, purification, crystallization and first structural data from microcrystalline specimens
Abstract
<jats:title>Abstract</jats:title><jats:p>Flavivirus infections often provoke life-threatening diseases of epidemic magnitudes, thus extensive research is currently directed towards the development of efficient vaccines and approved antiviral compounds. We present here the expression, purification, crystallization and preliminary X-ray diffraction analysis of one of the components of the flavivirus replication complex, the non-structural protein 5 (NS5) mRNA methyltransferase (MTase) domain, from an emerging pathogenic flavivirus, dengue virus 3 (DEN3). Polycrystalline precipitates of DEN3 NS5 MTase, suitable for X-ray powder diffraction (XRPD) measurements, were produced in the presence of PEG 8000 (25–32.5% (w/v)), 0.1 M Tris-Amino, in a pH range from 7.0 to 8.0. A polymorph of orthorhombic symmetry (space group:</jats:p>