<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Tetreau G</submitter><funding>U.S. Department of Health &amp;amp; Human Services | Centers for Disease Control and Prevention</funding><funding>Agence Nationale de la Recherche</funding><funding>NCRR NIH HHS</funding><funding>ACL HHS</funding><funding>Centre National de la Recherche Scientifique</funding><funding>DOE | Office of Science</funding><funding>U.S. Department of Health &amp;amp; Human Services | National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><funding>NCEZID CDC HHS</funding><pagination>4376</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9334358</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(1)</volume><pubmed_abstract>Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan, respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo-grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable cry</pubmed_abstract><journal>Nature communications</journal><pubmed_title>De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals.</pubmed_title><pmcid>PMC9334358</pmcid><funding_grant_id>1U01CK000516</funding_grant_id><funding_grant_id>U01 CK000516</funding_grant_id><funding_grant_id>P41GM103393</funding_grant_id><funding_grant_id>P41RR001209</funding_grant_id><funding_grant_id>ANR-17-EURE-0003</funding_grant_id><funding_grant_id>ANR-10-INBS-05-02</funding_grant_id><funding_grant_id>P41 RR001209</funding_grant_id><funding_grant_id>DE-AC02-76SF00515</funding_grant_id><funding_grant_id>R01 GM117126</funding_grant_id><funding_grant_id>P41 GM103393</funding_grant_id><funding_grant_id>T32 GM007185</funding_grant_id><funding_grant_id>PEPS SASLELX</funding_grant_id><funding_grant_id>NR-17-CE11-0018-01</funding_grant_id><funding_grant_id>GM117126</funding_grant_id><funding_grant_id>U01CK000516</funding_grant_id><funding_grant_id>ANR-2018-CE11-0005-02</funding_grant_id><pubmed_authors>Federici B</pubmed_authors><pubmed_authors>Doak RB</pubmed_authors><pubmed_authors>Bielecki J</pubmed_authors><pubmed_authors>Weik M</pubmed_authors><pubmed_authors>Schubert R</pubmed_authors><pubmed_authors>Canfield EJ</pubmed_authors><pubmed_authors>Kloos M</pubmed_authors><pubmed_authors>Hilpert M</pubmed_authors><pubmed_authors>Grunbein ML</pubmed_authors><pubmed_authors>Cascio D</pubmed_authors><pubmed_authors>Park HW</pubmed_authors><pubmed_authors>Shoeman RL</pubmed_authors><pubmed_authors>Riobe F</pubmed_authors><pubmed_authors>Brewster AS</pubmed_authors><pubmed_authors>Maury O</pubmed_authors><pubmed_authors>Schlichting I</pubmed_authors><pubmed_authors>Roux A</pubmed_authors><pubmed_authors>Teulon JM</pubmed_authors><pubmed_authors>De Zitter E</pubmed_authors><pubmed_authors>Banneville AS</pubmed_authors><pubmed_authors>Engilberge S</pubmed_authors><pubmed_authors>Bacia M</pubmed_authors><pubmed_authors>Burghammer M</pubmed_authors><pubmed_authors>de Wijn R</pubmed_authors><pubmed_authors>Tetreau G</pubmed_authors><pubmed_authors>Kovacs GN</pubmed_authors><pubmed_authors>Laporte F</pubmed_authors><pubmed_authors>Zala N</pubmed_authors><pubmed_authors>Qiao P</pubmed_authors><pubmed_authors>Pellequer JL</pubmed_authors><pubmed_authors>Coquelle N</pubmed_authors><pubmed_authors>Mancuso A</pubmed_authors><pubmed_authors>Young ID</pubmed_authors><pubmed_authors>Gutsche I</pubmed_authors><pubmed_authors>Batyuk A</pubmed_authors><pubmed_authors>Rodriguez J</pubmed_authors><pubmed_authors>Gorel A</pubmed_authors><pubmed_authors>Barends TRM</pubmed_authors><pubmed_authors>Despres L</pubmed_authors><pubmed_authors>Sauter NK</pubmed_authors><pubmed_authors>Colletier JP</pubmed_authors><pubmed_authors>Schibrowsky NA</pubmed_authors><pubmed_authors>Signor L</pubmed_authors><pubmed_authors>Ling WL</pubmed_authors><pubmed_authors>Bean R</pubmed_authors><pubmed_authors>Sierra RG</pubmed_authors><pubmed_authors>Alba MM</pubmed_authors><pubmed_authors>Sawaya MR</pubmed_authors><pubmed_authors>Schiro G</pubmed_authors><pubmed_authors>Snigireva I</pubmed_authors><pubmed_authors>Andreeva EA</pubmed_authors><pubmed_authors>Hunter MS</pubmed_authors><pubmed_authors>Fenel D</pubmed_authors><pubmed_authors>Sato T</pubmed_authors><pubmed_authors>Stricker M</pubmed_authors><pubmed_authors>Boutet S</pubmed_authors><pubmed_authors>Chapelle C</pubmed_authors><pubmed_authors>Foucar L</pubmed_authors><pubmed_authors>Kirkwood H</pubmed_authors><pubmed_authors>Letrun R</pubmed_authors><pubmed_authors>Laganowsky AD</pubmed_authors><pubmed_authors>Bideshi D</pubmed_authors><pubmed_authors>Girard E</pubmed_authors></additional><is_claimable>false</is_claimable><name>De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals.</name><description>Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan, respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo-grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable cry</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Jul</publication><modification>2026-05-28T01:11:30.67Z</modification><creation>2025-04-19T22:47:56.564Z</creation></dates><accession>S-EPMC9334358</accession><cross_references><pubmed>35902572</pubmed><doi>10.1038/s41467-022-31746-x</doi></cross_references></HashMap>