001047627 001__ 1047627 001047627 005__ 20251106202333.0 001047627 0247_ $$2doi$$aDOI: 10.1039/d5sm00181a 001047627 0247_ $$2doi$$a10.1039/d5sm00181a 001047627 0247_ $$2datacite_doi$$a10.34734/FZJ-2025-04427 001047627 037__ $$aFZJ-2025-04427 001047627 041__ $$aEnglish 001047627 082__ $$a530 001047627 1001_ $$0P:(DE-Juel1)184311$$aRay, Debes$$b0 001047627 245__ $$aElectric field-induced control of protein crystal morphology 001047627 260__ $$aLondon$$bRoyal Soc. of Chemistry$$c2025 001047627 3367_ $$2DRIVER$$aarticle 001047627 3367_ $$2DataCite$$aOutput Types/Journal article 001047627 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1762432568_32077 001047627 3367_ $$2BibTeX$$aARTICLE 001047627 3367_ $$2ORCID$$aJOURNAL_ARTICLE 001047627 3367_ $$00$$2EndNote$$aJournal Article 001047627 520__ $$aIn a previous study (D. Ray, et al., J. Phys. Chem. Lett., 2024, 15, 8108–8113), we found that an alternating electric field considerably affects the location of the crystallization boundary and the liquid–liquid phase separation line as well as crystallization kinetics in lysozyme solutions containing sodium thiocyanate(NaSCN). The present study extends this work by investigating the influence of the same electric field on the microscopic appearance of lysozyme crystals as they form from a supersaturated solution. We observe a variety of distinct crystal morphologies, which we classify as single- and multi-armcrystals, flower-like crystal structures, whiskers, and sea-urchin crystals. Crystal morphologies exhibit significant variations with changes in protein and salt concentrations, and the electric field strongly altersthe morphology-state diagram in the protein-versus-salt concentration plane. This alteration is likely due to the field effect on protein–protein interactions. We believe the effect is mediated by the field enhancedadsorption of SCN ions to the surface of lysozyme, ultimately driving the observed changes in crystallization behavior. These findings offer insights into how electric fields can be used to control crystal formation and morphology in protein systems. 001047627 536__ $$0G:(DE-HGF)POF4-5241$$a5241 - Molecular Information Processing in Cellular Systems (POF4-524)$$cPOF4-524$$fPOF IV$$x0 001047627 536__ $$0G:(GEPRIS)495795796$$aDFG project G:(GEPRIS)495795796 - Das Phasenverhalten von Proteinlösungen in elektrischen Feldern (495795796)$$c495795796$$x1 001047627 7001_ $$0P:(DE-Juel1)130749$$aKang, Kyongok$$b1$$eCorresponding author 001047627 7001_ $$0P:(DE-HGF)0$$aMadani$$b2 001047627 7001_ $$0P:(DE-Juel1)130616$$aDhont, Jan K. 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