Time-resolved structural investigations of crystallization of water in lipid/protein/salt mesophases at cryogenic temperatures are significant for comprehension of ice nanocrystal nucleation kinetics in lipid membranous systems and can lead to a better understanding of how to experimentally retard the ice formation that obstructs the protein crystal structure determination. Here, we present a time-resolved synchrotron microfocus X-ray diffraction (TR-XRD) study based on ∼40,000 frames that revealed the dynamics of water-to-ice crystallization in a lipid/protein/salt mesophase subjected to cryostream cooling at 100 K. The monoolein/hemoglobin/salt/water system was chosen as a model composition related to protein-loaded lipid cubic phases (LCP) broadly used for the crystallization of proteins. Under confinement in the nanoscale geometry, metastable short-living cubic ice (Ic) rapidly crystallized well before the formation of hexagonal ice (Ih). The detected early nanocrystalline states of water-to-ice transformation in multicomponent systems are relevant to a broad spectrum of technologies and understanding of natural phenomena, including crystallization, physics of water nanoconfinement, and rational design of anti-freezing and cryopreservation systems.

Institute of Physics ELI Beamlines Academy of Sciences of the Czech Republic CZ 18221 Prague Czech Republic

Institute of Physics ELI Beamlines Academy of Sciences of the Czech Republic CZ 18221 Prague Czech Republic; MFF Charles University CZ 12116 Prague Czech Republic

Synchrotron SOLEIL L'Orme des Merisiers Saint Aubin BP 48 F 91192 Gif sur Yvette France

Université Paris Saclay CNRS Institut Galien Paris Saclay F 91400 Orsay France

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