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Figure 6
Antifreeze properties and ice-binding site of FfIBP. (a) Ice crystals were grown in solutions of 4.2 µM FfIBP. Burst ice-crystal morphology was shown after the temperature dropped below the TH gap in the presence of recombinant FfIBP. (b) Inhibition of ice recrystallization by FfIBP. The first row shows RI assays using BSA protein (30 µM) as the negative control. The remaining rows show the RI activities of FfIBP at three different concentrations (134, 2.1 and 1.05 µM). (c) TH activity comparison of wild-type FfIBP and the mutants at 60 µM concentration. The location of each mutation in the FfIBP structure is labelled and shown as a stick model.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 70| Part 4| April 2014| Pages 1061-1073
https://doi.org/10.1107/S1399004714000996
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