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The single-stranded DNA-binding protein from M. tuberculosis has been crystallized in a trigonal form and an orthorhombic form. A mercury derivative of the trigonal crystals has been prepared.

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A comparative study involving the structures reported here and similar known structures show that the mobility of the UDG molecule consists of the rigid-body movement of the two domains that make up the molecule and the flexibility within the domains. DNA binding leads to domain closure, while association with the proteinaceous inhibitor does not.
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