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Compared to other forms of protein glycosylation, it is relatively uncommon but is affected by conformational anomalies and modeling errors similar to those seen in <jats:italic>N<\/jats:italic>\u2010 and <jats:italic>O<\/jats:italic>\u2010glycans in the Protein Data Bank (PDB). In this work, we report methods for detecting, building, and improving mannose structures linked to tryptophans. These methods have been used to mine X\u2010ray crystallographic and cryo\u2010electron microscopy maps in the PDB looking for unmodeled mannosylation, resulting in a number of cases where the modification can be placed in the map with high confidence. Additionally, we address most conformational issues affecting this modification. Finally, the development of a structural template to recognize thrombospondin repeats (TSR) domains where tryptophan mannosylation occurs will allow for the mannosylation of candidate\u2010predicted models, for example, those predicted with AlphaFold.<\/jats:p>","DOI":"10.1002\/pro.70025","type":"journal-article","created":{"date-parts":[[2025,1,22]],"date-time":"2025-01-22T12:05:26Z","timestamp":1737547526000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Methods for detecting, building, and improving tryptophan mannosylation in glycoprotein structures"],"prefix":"10.1002","volume":"34","author":[{"given":"Lou","family":"Holland","sequence":"first","affiliation":[{"name":"York Structural Biology Laboratory, Department of Chemistry University of York  York UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Phuong Thao","family":"Pham","sequence":"additional","affiliation":[{"name":"York 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