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The crystal structure of starch synthase I from barley was refined to 2.7 Å resolution. It includes a regulatory disulfide and a bound oligosaccharide. Activity assays were performed on several mutants.

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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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