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A method for experimental phasing by segmenting a large data set into sub-data sets for radiation-damage-induced phasing is presented.

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The crystal structure of endo-β-D-1,4-mannanase from Chrysonilia sitophila has been solved at 1.40 Å. The enzyme has mixed activity as both an endo-mannanase and endo-glucanase and the crystal structure revealed a unique arrangement of three surface loops surrounding the active site, altering the topography of the binding cleft.
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