biostudies-literatureGolub MEesti TeadusagentuurDeutsche Forschungsgemeinschaft8392-8405https://www.ebi.ac.uk/biostudies/studies/S-EPMC12376099biostudies-literatureUnknown129(33)Photosystems I (PSI) and II (PSII) are pigment-protein complexes that perform the light-driven charge separation necessary to convert solar energy into a biochemically usable form in a fundamental process called photosynthesis. Small-angle X-ray scattering provides unique structural insights into PSI and PSII in solution under near-physiological conditions. Here, we study the solubilization of PSI and PSII with different detergents, the octaethylene glycol monododecyl ether (C₁₂E₈) and the most commonly used n-dodecyl-β-D-maltoside (DDM). It is noteworthy that the volume of the C₁₂E₈ detergent belt is more compact for PSI and PSII than for DDM. Furthermore, circular dichroism measurements were used to detect thermal destabilization in protein solThe journal of physical chemistry. BDetergent Choice Shapes the Solution Structures of Photosystems I and II: Implications for Crystallization and High-Resolution Studies.PMC12376099SLOKT 12026TPRG 2772EXC 2008/1390540038SFB1078Blanchet CEGolub MHart OZouni APieper JGatcke JBoyka JWieland DCFHaupt SfalseDetergent Choice Shapes the Solution Structures of Photosystems I and II: Implications for Crystallization and High-Resolution Studies.Photosystems I (PSI) and II (PSII) are pigment-protein complexes that perform the light-driven charge separation necessary to convert solar energy into a biochemically usable form in a fundamental process called photosynthesis. Small-angle X-ray scattering provides unique structural insights into PSI and PSII in solution under near-physiological conditions. Here, we study the solubilization of PSI and PSII with different detergents, the octaethylene glycol monododecyl ether (C₁₂E₈) and the most commonly used n-dodecyl-β-D-maltoside (DDM). It is noteworthy that the volume of the C₁₂E₈ detergent belt is more compact for PSI and PSII than for DDM. Furthermore, circular dichroism measurements were used to detect thermal destabilization in protein sol2025-01-01T00:00:00Z2025 Aug2026-05-08T06:44:34.181Z2026-05-01T03:05:47.502ZS-EPMC123760994077970810.1021/acs.jpcb.5c00767