{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Golub M"],"funding":["Eesti Teadusagentuur","Deutsche Forschungsgemeinschaft"],"pagination":["8392-8405"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12376099"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["129(33)"],"pubmed_abstract":["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 (C<sub>12</sub>E<sub>8</sub>) and the most commonly used n-dodecyl-β-D-maltoside (DDM). It is noteworthy that the volume of the C<sub>12</sub>E<sub>8</sub> detergent belt is more compact for PSI and PSII than for DDM. Furthermore, circular dichroism measurements were used to detect thermal destabilization in protein sol"],"journal":["The journal of physical chemistry. B"],"pubmed_title":["Detergent Choice Shapes the Solution Structures of Photosystems I and II: Implications for Crystallization and High-Resolution Studies."],"pmcid":["PMC12376099"],"funding_grant_id":["SLOKT 12026T","PRG 2772","EXC 2008/1390540038","SFB1078"],"pubmed_authors":["Blanchet CE","Golub M","Hart O","Zouni A","Pieper J","Gatcke J","Boyka J","Wieland DCF","Haupt S"],"additional_accession":[]},"is_claimable":false,"name":"Detergent Choice Shapes the Solution Structures of Photosystems I and II: Implications for Crystallization and High-Resolution Studies.","description":"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 (C<sub>12</sub>E<sub>8</sub>) and the most commonly used n-dodecyl-β-D-maltoside (DDM). It is noteworthy that the volume of the C<sub>12</sub>E<sub>8</sub> detergent belt is more compact for PSI and PSII than for DDM. Furthermore, circular dichroism measurements were used to detect thermal destabilization in protein sol","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-05-08T06:44:34.181Z","creation":"2026-05-01T03:05:47.502Z"},"accession":"S-EPMC12376099","cross_references":{"pubmed":["40779708"],"doi":["10.1021/acs.jpcb.5c00767"]}}