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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography I04-1-Macromolecular Crystallography (fixed wavelength)	High-resolution structure of the alcohol dehydrogenase domain of the bifunctional bacterial enzyme AdhE Liyana Azmi , Eilis C. Bragginton , Ian T. Cadby , Olwyn Byron , Andrew Roe , Andrew L. Lovering , Mads Gabrielsen Acta Crystallographica Section F Structural Biology Communications 76, 414 - 421 DOI: 10.1107/S2053230X20010237 Diamond Proposal Number(s): [12112, 11651] Open Access Show Abstract ▼ Abstract: The bifunctional alcohol/aldehyde dehydrogenase (AdhE) comprises both an N-terminal aldehyde dehydrogenase (AldDH) and a C-terminal alcohol dehydrogenase (ADH). In vivo, full-length AdhE oligomerizes into long oligomers known as spirosomes. However, structural analysis of AdhE is challenging owing to the heterogeneity of the spirosomes. Therefore, the domains of AdhE are best characterized separately. Here, the structure of ADH from the pathogenic Escherichia coli O157:H7 was determined to 1.65 Å resolution. The dimeric crystal structure was confirmed in solution by small-angle X-ray scattering.	Sep 2020

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