{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T01:13:04Z","timestamp":1790817184412,"version":"4.1.0"},"reference-count":22,"publisher":"International Union of Crystallography (IUCr)","issue":"4","license":[{"start":{"date-parts":[[2023,3,30]],"date-time":"2023-03-30T00:00:00Z","timestamp":1680134400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"},{"start":{"date-parts":[[2023,3,30]],"date-time":"2023-03-30T00:00:00Z","timestamp":1680134400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"}],"funder":[{"DOI":"10.13039\/100007767","name":"National Institute of Standards and Technology, Material Measurement Laboratory","doi-asserted-by":"publisher","award":["016453295000"],"award-info":[{"award-number":["016453295000"]}],"id":[{"id":"10.13039\/100007767","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["iucr.org","wiley.com","iucrj.org"],"crossmark-restriction":true},"short-container-title":["Acta Crystallogr F Struct Biol Commun","Acta Crystallogr F","Acta Crystallogr F Struct Biol Cryst Commun","Acta Cryst F","Acta Cryst F Struct Biol Commun","Acta Cryst Sect F","Acta Cryst Sect F Struct Biol Commun","Acta Crystallogr Sect F","Acta Crystallogr Sect F Struct Biol Commun","Acta Crystallogr Sect F Struct Biol Cryst Commun"],"accepted":{"date-parts":[[2023,3,10]]},"published-print":{"date-parts":[[2023,4,1]]},"abstract":"<jats:p>\n                    CRM\n                    <jats:sub>197<\/jats:sub>\n                    is a genetically detoxified mutant of diphtheria toxin (DT) that is widely used as a carrier protein in conjugate vaccines. Protective immune responses to several bacterial diseases are obtained by coupling CRM\n                    <jats:sub>197<\/jats:sub>\n                    to glycans from these pathogens. Wild-type DT has been described in two oligomeric forms: a monomer and a domain-swapped dimer. Their proportions depend on the chemical conditions and especially the pH, with a large kinetic barrier to interconversion. A similar situation occurs in CRM\n                    <jats:sub>197<\/jats:sub>\n                    , where the monomer is preferred for vaccine synthesis. Despite 30 years of research and the increasing application of CRM\n                    <jats:sub>197<\/jats:sub>\n                    in conjugate vaccines, until now all of its available crystal structures have been dimeric. Here, CRM\n                    <jats:sub>197<\/jats:sub>\n                    was expressed as a soluble, intracellular protein in an\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    strain engineered to have an oxidative cytoplasm. The purified product, called EcoCRM, remained monomeric throughout crystallization. The structure of monomeric EcoCRM is reported at 2.0\u2005\u00c5 resolution with the domain-swapping hinge loop (residues 379\u2013387) in an extended, exposed conformation, similar to monomeric wild-type DT. The structure enables comparisons across expression systems and across oligomeric states, with implications for monomer\u2013dimer interconversion and for the optimization of conjugation.\n                  <\/jats:p>","DOI":"10.1107\/s2053230x23002364","type":"journal-article","created":{"date-parts":[[2023,3,22]],"date-time":"2023-03-22T09:33:16Z","timestamp":1679477596000},"page":"82-86","update-policy":"https:\/\/doi.org\/10.1107\/cm_01","source":"Crossref","is-referenced-by-count":7,"title":["Monomeric crystal structure of the vaccine carrier protein CRM\n                    <sub>197<\/sub>\n                    and implications for vaccine development"],"prefix":"10.1107","volume":"79","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1386-7255","authenticated-orcid":true,"given":"D. Travis","family":"Gallagher","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05xpvk416","id-type":"ROR","asserted-by":"publisher"}]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natalia","family":"Oganesyan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andrew","family":"Lees","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"329","published-online":{"date-parts":[[2023,3,30]]},"reference":[{"key":"jg5007_bb1","doi-asserted-by":"crossref","first-page":"1444","DOI":"10.1002\/pro.5560030911","volume":"3","author":"Bennett","year":"1994","journal-title":"Protein Sci."},{"key":"jg5007_bb2","doi-asserted-by":"crossref","first-page":"1464","DOI":"10.1002\/pro.5560030912","volume":"3","author":"Bennett","year":"1994","journal-title":"Protein Sci."},{"key":"jg5007_bb3","doi-asserted-by":"crossref","first-page":"11987","DOI":"10.1021\/acsomega.9b00418","volume":"4","author":"Bravo-Bautista","year":"2019","journal-title":"ACS Omega"},{"key":"jg5007_bb4","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.biologicals.2011.05.004","volume":"39","author":"Br\u00f6ker","year":"2011","journal-title":"Biologicals"},{"key":"jg5007_bb5","doi-asserted-by":"crossref","first-page":"2440","DOI":"10.1039\/D1SC01928G","volume":"13","author":"Carboni","year":"2022","journal-title":"Chem. 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Travis Gallagher\n                      et al.","order":0,"name":"copyright","label":"Copyright","explanation":{"URL":"https:\/\/journals.iucr.org\/services\/copyrightpolicy.html"},"group":{"name":"copyright_and_licencing","label":"Copyright and licencing"}},{"value":"Creative Commons Attribution (CC-BY)","order":1,"name":"license","label":"Licence","explanation":{"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/legalcode"},"group":{"name":"copyright_and_licencing","label":"Copyright and licencing"}}]}}