Liyana AzmiEilis C. BraggintonIan T. CadbyOlwyn ByronAndrew J. RoeAndrew L. LoveringMads Gabrielsen2024-05-272024-05-27202020/10/20202053-230X2409-1010.1107/S2053230X20010237https://journals.iucr.org/f/issues/2020/09/00/no5171/index.htmlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7470043/https://oarep.usim.edu.my/handle/123456789/3944Volume 76| Part 9| September 2020| Pages 414-421The 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. Keywords: alcohol dehydrogenase; AdhE; Escherichia colienalcohol dehydrogenase;AdhE;Escherichia colialcohol dehydrogenase domain of AdhE,6sci;NAD-bound,6scgArticle41442176