TY  - JOUR
AU  - Ray, Debes
AU  - Kang, Kyongok
AU  - Madani
AU  - Dhont, Jan K. G.
AU  - Platten, Florian
TI  - Electric field-induced control of protein crystal morphology
JO  - Soft matter
VL  - 21
SN  - 1744-683X
CY  - London
PB  - Royal Soc. of Chemistry
M1  - FZJ-2025-04427
SP  - 3012-3021
PY  - 2025
AB  - In 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.
LB  - PUB:(DE-HGF)16
DO  - DOI:10.1039/d5sm00181a
UR  - https://juser.fz-juelich.de/record/1047627
ER  -