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The human formylglycine-generating enzyme was cocrystallized with bromide and iodide ions, which, among other positions, occupy an oxygen-binding pocket that is crucial for enzyme catalysis. Halide ions may substitute for xenon in the detection of oxygen-binding sites.

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The crystal structure of orotidine-5′-monophosphate decarboxylase, the C-terminal domain of human UMP synthase, was determined by molecular replacement using data from highly pseudo-merohedrally twinned monoclinic crystals with ac unit-cell parameters.
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