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Craig J Marshall, Koli Basu, and Peter L Davies., Cryobiology, 2016.
The ‘ice shell’ is a new and effective method for purifying molecules, especially proteins, that interact with ice. These can be difficult to isolate because they tend to be very diverse and hard to separate from other proteins. One useful approach is to use the tendency of these proteins to attach to ice to separate them from everything else in a solution. An ‘ice finger’ has been used to do this for a number of years but this technique is slow and can process only about 100 mL of solution at a time. The ice shell uses the same principle as the ice finger: the controlled growth of ice to incorporate ice-active compounds while excluding almost everything else in the solution. The advantages of the ice shell are that it is much quicker and takes only a few hours rather than days, it can be scaled from 50 mL to several L, and it is more efficient than is the ice finger. The ice shell can be used for the rapid screening of ice active compounds in a wide range of samples including plant material, animal tissue including insects and fish, cultures of microorganisms, and environmental samples.