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The results observed for three different crystal forms of the enzyme PurE are reported and an attempt is made to infer some initial conclusions regarding the role that the solvent, the crystallization agents (mainly salts and polyethylene glycol) and interactions within the protein structures play in determining the changes in the diffraction pattern upon alteration of the external relative humidity of the crystals.

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The crystallographic structure of TrV shows specific morphological and functional features that clearly distinguish it from the type species of the Cripavirus genus, CrPV.

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Here, the re-refinement of the structure of the vault particle by incorporating the high-resolution information available for the R1-7 domains, using the deformable elastic network (DEN) approach and maintaining strict 39-fold noncrystallographic symmetry is reported.
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