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Using a combination of size\u2010exclusion chromatography coupled with multi\u2010angle light scattering (SEC\u2010MALS) and small\u2010angle scattering techniques (SAXS and SANS), we provide a detailed characterization of the protein\u2013detergent complex (PDC) behavior under varying conditions. Our results reveal that ShuA remains monomeric in 1% OPOE, whereas in 0.5\u2009mM DDM, it undergoes a reversible monomer\/dimer equilibrium that shifts towards a monodisperse, monomeric state with increasing DDM concentration to 7.5\u2009mM, highlighting the significant influence of detergent type and concentration on protein colloidal stability. These findings have direct implications for membrane protein purification and structural studies, particularly in crystallization and cryo\u2010EM sample preparation. The study emphasizes the necessity of optimizing detergent conditions to ensure monodispersity and structural integrity, preventing detergent\u2010induced artifacts that could affect structural interpretations. Importantly, our results highlight the power of the SEC\u2010MALS technique in determining oligomeric or association equilibrium states, detecting weak intermolecular interactions often overlooked in conventional SEC, and achieving this even in the particularly complex case of MPs. By integrating advanced scattering techniques, this work contributes valuable insights into MP colloidal behavior, refining strategies for structural characterization and providing a framework for optimizing detergent conditions in biochemical and biophysical studies.<\/jats:p>","DOI":"10.1002\/pro.70258","type":"journal-article","created":{"date-parts":[[2025,8,15]],"date-time":"2025-08-15T14:57:41Z","timestamp":1755269861000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Unraveling <scp>ShuA<\/scp> detergent\u2010induced colloidal behavior in solution: A comprehensive <scp>SEC<\/scp>\u2010<scp>MALS<\/scp>, <scp>SAXS,<\/scp> and <scp>SANS<\/scp> study"],"prefix":"10.1002","volume":"34","author":[{"given":"A.","family":"Pozza","sequence":"first","affiliation":[{"name":"Universit\u00e9 Paris Cit\u00e9, CNRS, Laboratoire de Biochimie des Prot\u00e9ines Membranaires Institut de Biologie Physico\u2010Chimique  Paris France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.","family":"Martel","sequence":"additional","affiliation":[{"name":"Large Scale Structures ILL Neutrons for Society, Institute Laue\u2010Langevin  Grenoble France"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"M.","family":"Moir","sequence":"additional","affiliation":[{"name":"National Deuteration Facility (NDF) Australian Nuclear Science and Technology Organization (ANSTO)  Lucas Heights New South Wales Australia"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T. 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