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The crystal structure of the putative mutarotase YeaD from S. typhimurium has been determined in orthorhombic and monoclinic crystal forms at 1.9 and 2.5 Å resolution, respectively. Comparison of the sequence and structure of YeaD with those of galactose mutarotases (GalMs) has allowed the identification of active-site residues and suggests plausible substrate specificity.

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The crystal structure of a recombinant triosephosphate isomerase (TIM) from the archaeabacterium M. jannaschii has been determined at a resolution of 2.3 Å using X-ray diffraction data from a tetartohedrally twinned crystal. M. jannaschii TIM (MjTIM) is tetrameric, as is the case for two other structurally characterized archaeal TIMs, and the unliganded structure has a completely disordered active-site loop.
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