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The crystal structure of B. subtilis RibG complexed with a deaminase product was determined and the yeast Rib2 structure was modelled. Subsequent mutational analysis was carried out to illustrate its distinct substrate specificity. An essential amino-binding hole which is conserved in the RNA/DNA-editing deaminases was also identified.

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The crystal structure of the dimeric R298A mutant of SARS-CoV Mpro offers insights into the molecular mechanism controlling monomer-dimer conversion during the process of Mpro maturation.
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