@article { ISI:A1996TT67400012,
	title = {Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase},
	journal = {NATURE STRUCTURAL BIOLOGY},
	volume = {3},
	number = {2},
	year = {1996},
	month = {FEB},
	pages = {149-154},
	abstract = {The three-dimensional structure of a catalytically competent glycosyl-enzyme intermediate of a retaining beta-1,4-glycanase has been determined at a resolution of 1.8 Angstrom by X-ray diffraction. A fluorinated slow substrate forms an alpha-D-glycopyranosyl linkage to one of the two invariant carboxylates, Glu 233, as supported in solution by F-19-NMR studies. The resulting ester linkage is coplanar with the cyclic oxygen of the proximal saccharide and is inferred to form a strong hydrogen bond with the 2-hydroxyl of that saccharide unit in natural substrates. The active-site architecture of this covalent intermediate gives insights into both the classical double-displacement catalytic mechanism and the basis for the enzyme{\textquoteright}s specificity.},
	issn = {1072-8368},
	doi = {10.1038/nsb0296-149},
	author = {White, A and TULL, D and Johns, K and Withers, SG and ROSE, DR}
}
