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The crystal structure of the metalloprotease Gentlyase is described and compared with the structures of other related thermolysin-like proteases.

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The first structure of a human β-galactoside α-2,6-sialyltransferase I was determined by SIRAS phasing using an iodide soak for derivatization. An elongated glycan from a crystallographic neighbour binds to the active site, mimicking a substrate complex. An analysis of the substrate interactions and a comparison with other sialyltransferases allowed the modelling of a Michaelis complex and conclusions on the catalytic mechanism.
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