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The crystal structures of a first fungal glycoside hydrolase family 5 β-mannosidase from Rhizomucor miehei (RmMan5B) and of its inactive E202A mutant in complex with mannobiose, mannotriose and mannosyl-fructose are presented. Structural analyses reveal the structural basis of substrates binding.

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Although urea and guanidine hydrochloride are commonly used to denature proteins, the molecular underpinnings of this process have remained unclear for a century. To address this question, crystal structures of β-catenin were determined at various urea concentrations.
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