Atmos. Chem. Phys., 20, 3291–3315, 2020 https://doi.org/10.5194/acp-20-3291-2020 © Author(s) 2020. This work is distributed under the Creative Commons Attribution 4.0 License. Protein aggregates nucleate ice: the example of apoferritin María Cascajo-Castresana1,2,3, Robert O. David3,4, Maiara A. Iriarte-Alonso2, Alexander M. Bittner2,5, and Claudia Marcolli3 1División de Salud, TECNALIA, Parque Tecnológico, Paseo de Mikeletegi, 2, 20009 Donostia, Spain 2CIC nanoGUNE, Tolosa Hiribidea, 76, 20018 Donostia, Spain 3Department of Environmental System Sciences, Institute for Atmospheric and Climate Science, ETH Zurich, 8092 Zurich, Switzerland 4Department of Geosciences, University of Oslo, Oslo, 0315, Norway 5Ikerbasque, Basque Foundation for Science, Ma Díaz de Haro 3, 48013 Bilbao, Spain Correspondence: Claudia Marcolli (
[email protected]) Received: 24 September 2019 – Discussion started: 7 October 2019 Revised: 10 February 2020 – Accepted: 17 February 2020 – Published: 20 March 2020 Abstract. Biological material has gained increasing atten- −4 to −11 ◦C and a lower one from −11 to −21 ◦C. Dy- tion recently as a source of ice-nucleating particles that may namic light scattering measurements related the upper freez- account for cloud glaciation at moderate supercooling. While ing range to ice-nucleating sites residing on aggregates and the ice-nucleation (IN) ability of some bacteria can be related the lower freezing range to sites located on misfolded cage to membrane-bound proteins with epitaxial fit to ice, little is monomers or oligomers. The sites proved to persist during known about the IN-active entities present in biological ma- several freeze–thaw cycles performed with the same sam- terial in general.