3.2.1.113	-	
3.2.1.113	crystals of both the native protein and the protein-inhibitor complex. Superimpositions are performed with LSQMAN. Comparison with human alpha-1,2-mannosidase–thiodisaccharide complex	
3.2.1.113	hanging drop vapor diffusion method, 15 A resolution	
3.2.1.113	in complex with kifunensine	
3.2.1.113	in complex with the substrate analogue methyl-alpha-D-lyxopyranosyl-(1',2)-alpha-D-mannopyranoside, to 1.95 A resolution. The intact disaccharide spans the ?1/+1 subsites, with the D-lyxoside ring in the -1 subsite in the 1C4 chair conformation.The absence of the C5' hydroxymethyl group on the D-lyxoside moiety results in the side chain of Arg407 adopting two alternative conformations, the minor one interacting with Asp375 and the major one interacting with both the D-lyxoside and the catalytic base Glu409, thus disrupting its function	
3.2.1.113	modeling of structure at 2.2 A resolution	
3.2.1.113	native enzyme and in complexes with the inhibitors 1-deoxymannojirimycin and kifunensine, hanging drop vapor diffusion method, using 17-22% (w/v) polyethylene glycol 6000, 50 mM KH2PO4, pH 4.6