  Concentrated aqueous solutions of the protein lysozyme undergo a liquid solid
transition upon a temperature quench into the unstable spinodal region below a
characteristic arrest temperature of Tf=15C. We use video microscopy and
ultra-small angle light scattering in order to investigate the arrested
structures as a function of initial concentration, quench temperature and rate
of the temperature quench. We find that the solid-like samples show all the
features of a bicontinuous network that is formed through an arrested spinodal
decomposition process. We determine the correlation length Xi and demonstrate
that Xi exhibits a temperature dependence that closely follows the critical
scaling expected for density fluctuations during the early stages of spinodal
decomposition. These findings are in agreement with an arrest scenario based on
a state diagram where the arrest or gel line extends far into the unstable
region below the spinodal line. Arrest then occurs when during the early stage
of spinodal decomposition the volume fraction phi2 of the dense phase
intersects the dynamical arrest threshold phi2Glass, upon which phase
separation gets pinned into a space-spanning gel network with a characteristic
length Xi.
