Conformational variation of proteins at room temperature is not dominated by radiation damage.

A linear fit of 1 − S 2 , averaged over all residues, against dose indicates a highly significant increase in disorder at 100 K from lowest to highest radiation dose: around 20% for thaumatin ( p < 0.005) and around 35% for CypA ( p < 10 −6 ) between the first and last dataset in the series.

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Although it was not possible to discern a clear trend between damage and multiple conformations at either temperature, it was observed that disorder, monitored by B -factor-dependent crystallographic order parameters, increased with higher absorbed dose for the three proteins at 100 K.

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There is a decreasing trend for the total number of conformations as a function of dose for all three proteins at 278 K, but these trends are not statistically significant.

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