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Abstract The Eulerian multifluid mathematical model is developed to describe the marine atmospheric boundary layer laden with sea spray under the high-wind condition of a hurricane. The model considers spray and air as separate continuous interacting turbulent media and employs the multifluid E –ϵ closure. Each phase is described by its own set of coupled conservation equations and characterized by its own velocity. Such an approach enables us to accurately quantify the interaction between spray and air and pinpoint the effect of spray on the vertical momentum transport much more precisely than could be done with traditional mixture-type approaches. The model consistently quantifies the effect of spray inertia and the suppression of air turbulence due to two different mechanisms: the turbulence attenuation, which results from the inability of spray droplets to fully follow turbulent fluctuations, and the vertical transport of spray against the gravity by turbulent eddies. The results of numerical and asymptotic analyses show that the turbulence suppression by spray overpowers its inertia several meters above wave crests, resulting in a noticeable wind acceleration and the corresponding reduction of the drag coefficient from the reference values for a spray-free atmosphere. This occurs at much lower than predicted previously spray volume fraction values of ∼10 −5 . The falloff of the drag coefficient from its reference values is more strongly pronounced at higher altitudes. The drag coefficient reaches its maximum at spray volume fraction values of ∼10 −4 , which is several times smaller than predicted by mixture-type models. 

Abstract Bacteria encode myriad defences that target the genomes of infecting bacteriophage, including restriction–modification and CRISPR–Cas systems 1 . In response, one family of large bacteriophages uses a nucleus-like compartment to protect its replicating genomes by excluding host defence factors 2–4 . However, the principal composition and structure of this compartment remain unknown. Here we find that the bacteriophage nuclear shell assembles primarily from one protein, which we name chimallin (ChmA). Combining cryo-electron tomography of nuclear shells in bacteriophage-infected cells and cryo-electron microscopy of a minimal chimallin compartment in vitro, we show that chimallin self-assembles as a flexible sheet into closed micrometre-scale compartments. The architecture and assembly dynamics of the chimallin shell suggest mechanisms for its nucleation and growth, and its role as a scaffold for phage-encoded factors mediating macromolecular transport, cytoskeletal interactions, and viral maturation.