{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T16:59:30Z","timestamp":1790441970671,"version":"4.1.0"},"reference-count":33,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2027,1,1]],"date-time":"2027-01-01T00:00:00Z","timestamp":1798761600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100013076","name":"National Major Science and Technology Projects of China","doi-asserted-by":"publisher","award":["2026ZD1218801"],"award-info":[{"award-number":["2026ZD1218801"]}],"id":[{"id":"10.13039\/501100013076","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Protein Expression and Purification"],"published-print":{"date-parts":[[2027,1]]},"DOI":"10.1016\/j.pep.2026.106997","type":"journal-article","created":{"date-parts":[[2026,8,27]],"date-time":"2026-08-27T06:59:48Z","timestamp":1787813988000},"page":"106997","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["An optimized high-pH solubilization strategy for efficient purification and functional recovery of E. coli-expressed Cry toxins"],"prefix":"10.1016","volume":"243","author":[{"given":"Zibo","family":"Cui","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lianlian","family":"Cui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaiyue","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liru","family":"Liu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1097-7283","authenticated-orcid":false,"given":"Sheng","family":"Ye","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.pep.2026.106997_bib1","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1016\/j.ceb.2009.04.003","article-title":"Membrane injury by pore-forming proteins","volume":"21","author":"Bischofberger","year":"2009","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.pep.2026.106997_bib2","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.pbiomolbio.2004.01.009","article-title":"Pore-forming protein toxins: from structure to function","volume":"88","author":"Parker","year":"2005","journal-title":"Prog. Biophys. Mol. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib3","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.sbi.2010.01.013","article-title":"Structure and assembly of pore-forming proteins","volume":"20","author":"Iacovache","year":"2010","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib4","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.3390\/toxins6082393","article-title":"Molecular approaches to improve the insecticidal activity of Bacillus thuringiensis cry toxins","volume":"6","author":"Lucena","year":"2014","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.pep.2026.106997_bib5","doi-asserted-by":"crossref","first-page":"2732","DOI":"10.3390\/toxins6092732","article-title":"Structural insights into Bacillus thuringiensis cry, cyt and parasporin toxins","volume":"6","author":"Xu","year":"2014","journal-title":"Toxins"},{"key":"10.1016\/j.pep.2026.106997_bib6","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1751-7915.2012.00342.x","article-title":"Evolution of Bacillus thuringiensis cry toxins insecticidal activity","volume":"6","author":"Bravo","year":"2013","journal-title":"Microb. Biotechnol."},{"key":"10.1016\/j.pep.2026.106997_bib7","doi-asserted-by":"crossref","first-page":"423","DOI":"10.1016\/j.ibmb.2011.02.006","article-title":"Bacillus thuringiensis: a story of a successful bioinsecticide","volume":"41","author":"Bravo","year":"2011","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib8","doi-asserted-by":"crossref","first-page":"317","DOI":"10.3109\/07388551.2014.960793","article-title":"Bacillus thuringiensis: mechanism of action, resistance, and new applications: a review","volume":"36","author":"Melo","year":"2016","journal-title":"Crit. Rev. Biotechnol."},{"key":"10.1016\/j.pep.2026.106997_bib9","doi-asserted-by":"crossref","first-page":"12497","DOI":"10.1074\/jbc.M109.085266","article-title":"Role of alkaline phosphatase from Manduca sexta in the mechanism of action of Bacillus thuringiensis Cry1Ab toxin","volume":"285","author":"Arenas","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2026.106997_bib10","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1574-6976.2012.00341.x","article-title":"Bacillus thuringiensis insecticidal three-domain cry toxins: mode of action, insect resistance and consequences for crop protection","volume":"37","author":"Pardo-Lopez","year":"2013","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.pep.2026.106997_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.jip.2020.107438","article-title":"A structure-based nomenclature for Bacillus thuringiensis and other bacteria-derived pesticidal proteins","volume":"186","author":"Crickmore","year":"2021","journal-title":"J. Invertebr. Pathol."},{"key":"10.1016\/j.pep.2026.106997_bib12","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1007\/s00018-008-8330-9","article-title":"Signaling versus punching hole: how do Bacillus thuringiensis toxins kill insect midgut cells?","volume":"66","author":"Sober\u00f3n","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.pep.2026.106997_bib13","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jip.2012.05.001","article-title":"Current models of the mode of action of Bacillus thuringiensis insecticidal crystal proteins: a critical review","volume":"111","author":"Vachon","year":"2012","journal-title":"J. Invertebr. Pathol."},{"key":"10.1016\/j.pep.2026.106997_bib14","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1128\/MMBR.00034-06","article-title":"Role of receptors in Bacillus thuringiensis crystal toxin activity","volume":"71","author":"Pigott","year":"2007","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.pep.2026.106997_bib15","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1002\/pro.3561","article-title":"Crystal structure of Bacillus thuringiensis Cry7Ca1 toxin active against Locusta migratoria manilensis","volume":"28","author":"Jing","year":"2019","journal-title":"Protein Sci."},{"key":"10.1016\/j.pep.2026.106997_bib16","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4419-6327-7_1","article-title":"Proteins: membrane binding and pore formation. Introduction","volume":"677","author":"Feil","year":"2010","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib17","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/j.peptides.2008.08.006","article-title":"Enhancement of insecticidal activity of Bacillus thuringiensis Cry1A toxins by fragments of a toxin-binding cadherin correlates with oligomer formation","volume":"30","author":"Pacheco","year":"2009","journal-title":"Peptides"},{"key":"10.1016\/j.pep.2026.106997_bib18","doi-asserted-by":"crossref","first-page":"1640","DOI":"10.1126\/science.1146453","article-title":"Engineering modified Bt toxins to counter insect resistance","volume":"318","author":"Soberon","year":"2007","journal-title":"Science"},{"key":"10.1016\/j.pep.2026.106997_bib19","doi-asserted-by":"crossref","first-page":"20793","DOI":"10.1074\/jbc.M114.627554","article-title":"Potential prepore trimer formation by the Bacillus thuringiensis mosquito-specific toxin","volume":"290","author":"Sriwimol","year":"2015","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pep.2026.106997_bib20","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1002\/jat.3252","article-title":"An overview of the safety and biological effects of Bacillus thuringiensis cry toxins in mammals","volume":"36","author":"Rubio-Infante","year":"2016","journal-title":"J. Appl. Toxicol."},{"key":"10.1016\/j.pep.2026.106997_bib21","first-page":"5","article-title":"Recombinant protein expression in escherichia coli: advances and challenges","author":"Rosano","year":"2014","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.pep.2026.106997_bib22","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1186\/s13568-021-01270-0","article-title":"Key residues of Bacillus thuringiensis Cry2Ab for oligomerization and pore-formation activity","volume":"11","author":"Pan","year":"2021","journal-title":"AMB Express"},{"key":"10.1016\/j.pep.2026.106997_bib23","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/nprot.2017.094","article-title":"Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR","volume":"13","author":"Hagn","year":"2018","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.pep.2026.106997_bib24","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.jsb.2006.05.009","article-title":"EMAN2: an extensible image processing suite for electron microscopy","volume":"157","author":"Tang","year":"2007","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib25","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","article-title":"RELION: implementation of a Bayesian approach to cryo-EM structure determination","volume":"180","author":"Scheres","year":"2012","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib26","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1007\/BF00250449","article-title":"Behavior of Bacillus thuringiensis var. kurstaki under continuous phased cultivation in a cyclone fermentor","volume":"28","author":"Selinger","year":"1988","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.pep.2026.106997_bib27","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.pep.2004.02.016","article-title":"Optimised expression in Escherichia coli and purification of the functional form of the Bacillus thuringiensis Cry4Aa \u03b4-endotoxin","volume":"35","author":"Boonserm","year":"2004","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.pep.2026.106997_bib28","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.ibmb.2016.07.008","article-title":"Three toxins, two receptors, one mechanism: mode of action of Cry1A toxins from Bacillus thuringiensis in Heliothis virescens","volume":"76","author":"Bretschneider","year":"2016","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pep.2026.106997_bib29","doi-asserted-by":"crossref","DOI":"10.3390\/biom14040425","article-title":"Utilization of diverse molecules as receptors by cry toxin and the promiscuous nature of receptor-binding sites which accounts for the diversity","volume":"14","author":"Sato","year":"2024","journal-title":"Biomolecules"},{"key":"10.1016\/j.pep.2026.106997_bib30","doi-asserted-by":"crossref","first-page":"1492","DOI":"10.1002\/ps.6170","article-title":"Two ABC transporters are differentially involved in the toxicity of two Bacillus thuringiensis Cry1 toxins to the invasive crop-pest Spodoptera frugiperda (J. E. Smith)","volume":"77","author":"Jin","year":"2021","journal-title":"Pest Manag. Sci."},{"key":"10.1016\/j.pep.2026.106997_bib31","doi-asserted-by":"crossref","first-page":"7209","DOI":"10.1007\/s00253-015-6755-2","article-title":"Assembling of Holotrichia parallela (dark black chafer) midgut tissue transcriptome and identification of midgut proteins that bind to Cry8Ea toxin from Bacillus thuringiensis","volume":"99","author":"Shu","year":"2015","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.pep.2026.106997_bib32","doi-asserted-by":"crossref","DOI":"10.1016\/j.pep.2023.106320","article-title":"Optimized high-yield preparation of alkaline-solubilizable crystalline inclusion of the Bacillus thuringiensis Cry4Aa \u03b4-endotoxin expressed in Escherichia coli","volume":"210","author":"Sakdee","year":"2023","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.pep.2026.106997_bib33","doi-asserted-by":"crossref","DOI":"10.3390\/toxins14070433","article-title":"Molecular and kinetic models for pore formation of Bacillus thuringiensis cry toxin","volume":"14","author":"Endo","year":"2022","journal-title":"Toxins (Basel)"}],"container-title":["Protein Expression and Purification"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592826001208?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1046592826001208?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T16:32:03Z","timestamp":1790440323000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1046592826001208"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2027,1]]},"references-count":33,"alternative-id":["S1046592826001208"],"URL":"https:\/\/doi.org\/10.1016\/j.pep.2026.106997","relation":{},"ISSN":["1046-5928"],"issn-type":[{"value":"1046-5928","type":"print"}],"subject":[],"published":{"date-parts":[[2027,1]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"An optimized high-pH solubilization strategy for efficient purification and functional recovery of E. coli-expressed Cry toxins","name":"articletitle","label":"Article Title"},{"value":"Protein Expression and Purification","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.pep.2026.106997","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"106997"}}