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. 2017 Nov 16;8:1546. doi: 10.1038/s41467-017-01421-7

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — Interaction of antifreeze proteins with ice. a Hexagonal ice crystal; b Adsorption-inhibition where AF(G)Ps bind to ice, causing local curvature and hence growth inhibition; c Preferential c-axis (basal) growth when prism planes inhibited; d Different morphologies observed for single ice crystals; e Micrographs of ice crystals after annealing with/without antifreeze proteins showing IRI activity; f TH activity for different molecular weight AFGPs (2.6–24 kDa)^{4, 33}. a–d are reproduced from Gibson (2010)²⁴ with permission of The Royal Society of Chemistry. These images are not included under the creative commons licence for this article. f was created using the raw data from Wu et al. (2001)³³