| 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
Unit-cell response of tetragonal hen egg white lysozyme upon controlled relative humidity variation
Abstract
<jats:p>Variation of relative humidity (rH) greatly affects the internal order of solvent-based protein crystals, and the rearrangement of molecules can be efficiently recorded in distinct diffraction patterns. This study focuses on this topic, reporting the effect of rH variation experiments on hen egg white lysozyme (HEWL) polycrystalline precipitates of tetragonal symmetry using X-ray powder diffraction (XRPD). <jats:italic>In situ</jats:italic> XRPD data were collected on HEWL specimens during dehydration and rehydration processes using laboratory instrumentation. A known polymorph [space group <jats:italic>P</jats:italic>4<jats:sub>3</jats:sub>2<jats:sub>1</jats:sub>2, <jats:italic>a</jats:italic> = 79.07181 (1), <jats:italic>c</jats:italic> = 38.0776 (1) Å] was identified during gradual dehydration from 95 to 63% rH and vice versa. Pawley analysis of collected data sets and accurate extraction of unit-cell parameters indicated a characteristic evolution of the tetragonal axes with rH. In addition, there is a low humidity level below which samples do not retain their crystallinity. This work illustrates the accuracy of laboratory XRPD as a probe for time-resolved studies of proteins and <jats:italic>in situ</jats:italic> investigations of gradual structural modifications upon rH variation. These experiments provide essential information for improving production and post-production practices of microcrystalline protein-based pharmaceuticals.</jats:p>