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Instruments / Technical Area	Publication Details	Published	Actions
I02-Macromolecular Crystallography I03-Macromolecular Crystallography I24-Microfocus Macromolecular Crystallography	Structural and functional insight into human O-GlcNAcase Christian Roth , Sherry Chan , Wendy A. Offen , Glyn R. Hemsworth , Lianne I. Willems , Dustin T. King , Vimal Varghese , Robert Britton , David J. Vocadlo , Gideon J. Davies Nature Chemical Biology 258 DOI: 10.1038/nchembio.2358 Diamond Proposal Number(s): [1221, 7864, 9948] Show Abstract ▼ Abstract: O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value.	Mar 2017

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