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Various aerosols, including mineral dust, soot, and biological particles, can act as ice nuclei, initiating the freezing of supercooled cloud droplets. Cloud droplet freezing significantly impacts cloud properties and, consequently, weather and climate. Some biological ice nuclei exhibit exceptionally high nucleation temperatures close to 0 °C. Ice-nucleating macromolecules (INMs) found on pollen are typically not considered among the most active ice nuclei. Still, they can be highly abundant, especially for species such as Betula pendula, a widespread birch tree species in the boreal forest. Recent studies have shown that certain tree-derived INMs exhibit ice nucleation activity above −10 °C, suggesting they could play a more significant role in atmospheric processes than previously understood. Our study reveals that three distinct INM classes active at −8.7, −15.7, and −17.4 °C are present in B. pendula. Freeze drying and freeze–thaw cycles noticeably alter their ice nucleation capability, and the results of heat treatment, size, and chemical analysis indicate that INM classes correspond to size-varying aggregates, with larger aggregates nucleating ice at higher temperatures, in agreement with previous studies on fungal and bacterial ice nucleators. Our findings suggest that B. pendula INMs are potentially important for atmospheric ice nucleation because of their high prevalence and nucleation temperatures. 

Biological ice nucleation plays a key role in the survival of cold-adapted organisms. Several species of bacteria, fungi, and insects produce ice nucleators (INs) that enable ice formation at temperatures above −10 °C. Bacteria and fungi produce particularly potent INs that can promote water crystallization above −5 °C. Bacterial INs consist of extended protein units that aggregate to achieve superior functionality. Despite decades of research, the nature and identity of fungal INs remain elusive. Here, we combine ice nucleation measurements, physicochemical characterization, numerical modeling, and nucleation theory to shed light on the size and nature of the INs from the fungusFusarium acuminatum. We find ice-binding and ice-shaping activity ofFusariumIN, suggesting a potential connection between ice growth promotion and inhibition. We demonstrate that fungal INs are composed of small 5.3 kDa protein subunits that assemble into ice-nucleating complexes that can contain more than 100 subunits.FusariumINs retain high ice-nucleation activity even when only the ~12 kDa fraction of size-excluded proteins are initially present, suggesting robust pathways for their functional aggregation in cell-free aqueous environments. We conclude that the use of small proteins to build large assemblies is a common strategy among organisms to create potent biological INs.