Structure and stability of self-assembled actin-lysozyme complexes in   salty water
  Interactions between actin, an anionic polyelectrolyte, and lysozyme, a cationic globular protein, have been examined using a combination of synchrotron small-angle x-ray scattering and molecular dynamics simulations. Lysozyme initially bridges pairs of actin filaments, which relax into hexagonally-coordinated columnar complexes comprised of actin held together by incommensurate one-dimensional close-packed arrays of lysozyme macroions. These complexes are found to be stable even in the presence of significant concentrations of monovalent salt, which is quantitatively explained from a redistribution of salt between the condensed and the aqueous phases. 
Lori K. Sanders, Camilo Guaqueta, Thomas E. Angelini, Jae-Wook Lee,   Scott C. Slimmer, Erik Luijten, Gerard C.L. Wong