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These include studies on high\u2010resolution structures of human acetylcholinesterase and its complexes; the first crystal structure of a snake venom acetylcholinesterase, in which open and closed states of the \u2018back door\u2019 are visualized; a powerful algorithm for redesigning proteins for enhanced expression in prokaryotic systems, as applied to human acetylcholinesterase, which has hitherto been an intractable target;<jats:italic>in\u00a0situ<\/jats:italic>implementation of \u2018click chemistry\u2019 in crystalline acetylcholinesterase, which yields novel insights into the steric and dynamic changes involved in the reaction within the active\u2010site gorge; and a study that demonstrates the effect of crystallization conditions on ligand alignment within a protein complex, in this case the methylene blue\u2013<jats:italic>Torpedo californica<\/jats:italic>acetylcholinesterase complex, which highlights the relevance of the precipitant employed to structure\u2010based drug design.<\/jats:p><jats:p><jats:bold>This is an article for the<\/jats:bold>\u00a0<jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/onlinelibrary.wiley.com\/journal\/10.1111\/(ISSN)1471-4159\/homepage\/special_issues.htm\">special issue XVth International Symposium on Cholinergic Mechanisms<\/jats:ext-link>.<\/jats:p><\/jats:sec><jats:sec><jats:label\/><jats:p><jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc13992-fig-0006-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text><\/jats:p><\/jats:sec>","DOI":"10.1111\/jnc.13992","type":"journal-article","created":{"date-parts":[[2017,5,15]],"date-time":"2017-05-15T08:56:45Z","timestamp":1494838605000},"page":"19-25","source":"Crossref","is-referenced-by-count":34,"title":["Recent developments in structural studies on acetylcholinesterase"],"prefix":"10.1111","volume":"142","author":[{"given":"Israel","family":"Silman","sequence":"first","affiliation":[{"name":"Department of Neurobiology Weizmann Institute of Science Rehovot Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joel L.","family":"Sussman","sequence":"additional","affiliation":[{"name":"Department of Structural Biology Weizmann Institute of Science Rehovot Israel"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2017,5,15]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi401043w"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/cdg005"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.0308206100"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja106820e"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M114.603902"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1021\/jacs.5b11384"},{"key":"e_1_2_9_8_1","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/S0026-895X(24)23214-4","article-title":"Huprine X is a novel high\u2010affinity inhibitor of acetylcholinesterase that is of interest for treatment of Alzheimer's disease","volume":"57","author":"Camps P.","year":"2000","journal-title":"Mol. 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