{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"institution":[{"name":"bioRxiv"}],"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T21:19:43Z","timestamp":1792790383562,"version":"4.5.0"},"posted":{"date-parts":[[2026,6,18]]},"group-title":"Biophysics","reference-count":47,"publisher":"openRxiv","license":[{"start":{"date-parts":[[2026,6,18]],"date-time":"2026-06-18T00:00:00Z","timestamp":1781740800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"NINDS","award":["NS095892"],"award-info":[{"award-number":["NS095892"]}],"id":[{"id":"https:\/\/ror.org\/01s5ya894","id-type":"ROR","asserted-by":"crossref"}]},{"name":"NIDDK","award":["DK046335"],"award-info":[{"award-number":["DK046335"]}],"id":[{"id":"https:\/\/ror.org\/00adh9b73","id-type":"ROR","asserted-by":"crossref"}]},{"name":"German Research Council","award":["556478029"],"award-info":[{"award-number":["556478029"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"accepted":{"date-parts":[[2026,9,14]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                <jats:p>Amyloid fibrils extracted from patient tissue are enriched by physico-chemical fractionation methods and enzymatic tissue digestion with collagenase, resulting in a mixture of sedimented complexes. Reprocessing of an ex vivo lysozyme amyloid dataset revealed non-amyloid tubular assemblies, which we reconstructed to 3.5 \u00c5. Sequence-agnostic model building with CryoAtom and fold search with FoldSeek identified a phage tail tube fold. Testing the crude Clostridium histolyticum collagenase used for tissue digestion, negative-stain TEM and LC-MS\/MS showed proteins of an F-type tailocin, allowing us to assign the helical reconstruction to a major tail tube protein (TTP) of C. histolyticum. We also observed tailocin contamination in cardiac light-chain amyloid extracts, following the same collagenase treatment. Overall, we identify tailocins as recurrent reagent-borne contaminants in collagenase-treated ex vivo amyloid preparations and propose strategies to detect and avoid such artefacts in single-particle cryo-EM by optimizing the experimental design and data annotation towards a database of common contaminants.<\/jats:p>\n                <jats:sec>\n                  <jats:title>Abstract Figure<\/jats:title>\n                  <jats:fig id=\"ufig1\" position=\"float\" fig-type=\"figure\" orientation=\"portrait\">\n                    <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"733002v2_ufig1\" position=\"float\" orientation=\"portrait\"\/>\n                  <\/jats:fig>\n                <\/jats:sec>","DOI":"10.64898\/2026.06.17.733002","type":"posted-content","created":{"date-parts":[[2026,6,19]],"date-time":"2026-06-19T06:05:17Z","timestamp":1781849117000},"source":"Crossref","is-referenced-by-count":0,"title":["Tailocins are recurrent contaminants in ex 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