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@ARTICLE{Kang:1049215,
      author       = {Kang, Kyongok and Platten, Florian and Ray, Debes},
      title        = {{E}lectric response of multiarm protein crystals},
      journal      = {Physical review / E},
      volume       = {113},
      issn         = {2470-0045},
      address      = {Woodbury, NY},
      publisher    = {APS},
      reportid     = {FZJ-2025-05295},
      pages        = {014403},
      year         = {2026},
      abstract     = {Electric fields can modify protein-protein interactions and
                      thereby influence phase behavior. In lysozyme–sodium
                      thiocyanate solutions, we recently observed shifts in both
                      the crystallization boundary and theliquid-liquid phase
                      separation line under a weak applied field, along with a
                      range of distinct crystal morphologies.Here, we explore how
                      forming protein crystals respond to variations in field
                      frequency and amplitude, focusingon the morphologies of
                      complex, multiarm structures. At constant protein and salt
                      concentrations, the appliedfield governs both the number and
                      the angular distribution of crystal arms. These features are
                      analyzed throughFourier analysis of microscopy images,
                      revealing cooperative angular ordering among the arms. Based
                      on theseobservations, we classify three principal multiarm
                      protein crystal (pX) morphologies: flowerlike pX (dominantat
                      high field strengths), triconic pX (appearing
                      nonmonotonically at lower fields), and conic pX (widely
                      observedunder low-field conditions). Near the
                      crystallization boundary, field-driven metastable structures
                      such as tubules,clusters, nematic domains, and fibers also
                      occur in response to the field. These findings demonstrate
                      that electricfields effectively steer protein
                      crystallization pathways and provide insight into the
                      mechanisms of variousmultiarm crystallization.},
      cin          = {IBI-4},
      ddc          = {530},
      cid          = {I:(DE-Juel1)IBI-4-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / DFG project G:(GEPRIS)495795796 - Das
                      Phasenverhalten von Proteinlösungen in elektrischen Feldern
                      (495795796)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)495795796},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1103/ql7f-wzpr},
      url          = {https://juser.fz-juelich.de/record/1049215},
}