Nuclear magnetic resonance relaxation time measurements are reported for monoclinic lysozyme crystals. The data require three proton populations including two proton populations associated with the protein surface. One of the surface populations exchanges rapidly with the interior aqueous solution of the crystal, the other does not. The data are analyzed assuming a log normal distribution of correlation times for each unaveraged relaxation component. It is concluded that a significant fraction of the water in a protein crystal is essentially liquid and that the distances over which the protein perturbs the dynamic aspects of water structure are short.
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