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Stress-induced recrystallization of a protein crystal by electron irradiation


Ordering of a system of particles into its thermodynamically stable state usually proceeds by thermally activated mass transport of its constituents. Particularly at low temperature, the activation barrier often hinders equilibration—this is what prevents a glass from crystallizing1 and a pile of sand from flattening under gravity. But if the driving force for mass transport (that is, the excesss energy of the system) is increased, the activation barrier can be overcome and structural changes are initiated2. Here we report the reordering of radiation-damaged protein crystals under conditions where transport is initiated by stress rather than by thermal activation. After accumulating a certain density of radiation-induced defects during observation by transmission electron microscopy, the distorted crystal recrystallizes. The reordering is induced by stress caused by the defects at temperatures that are low enough to suppress diffusive mass transport. We propose that this defect-induced reordering might be a general phenomenon.

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Figure 1: Sequence of TEM images of a protein crystal.
Figure 2: Time dependence of autocorrelation, short-range order and contrast of Fig. 1
Figure 3: Electron diffraction images of a protein crystal under progressing irradiation.
Figure 4: Recrystallization of a soap bubble ‘crystal’.

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The authors thank R. Schlögl and W. Storck for continuous support and fruitful discussions.

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Correspondence to R. Schuster.

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Zemlin, F., Schuster, R., Beckmann, E. et al. Stress-induced recrystallization of a protein crystal by electron irradiation. Nature 399, 51–54 (1999).

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