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A case study on the treatment of SIRAS data using the originally unknown protein LegC3N is described. An iterative direct-method-based treatment was proposed that led to improved results in this particular test case.

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The crystal structure of a bacterial acetyltransferase with 27% sequence identity to the C-terminal domain of human O-GlcNAcase has been solved at 1.5 Å resolution. This S. sviceus protein is compared with known GCN5-related acetyltransferases, adding to the diversity observed in this superfamily.
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