{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Brady NG"],"funding":["University of Tennessee, Knoxville","Office of Cyberinfrastructure","Division of Molecular and Cellular Biosciences","Office of Experimental Program to Stimulate Competitive Research","Oak Ridge National Laboratory","Division of Graduate Education"],"pagination":["31781-31796"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9072662"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(54)"],"pubmed_abstract":["Photosystem I (PSI) from the thermophilic cyanobacterium <i>Thermosynechococcus elongatus</i> (Te) is the largest membrane protein complex to have had its structure solved by X-ray diffraction. This trimeric complex has 36 protein subunits, over 380 non-covalently bound cofactors and a molecular weight of ∼1.2 MDa. Previously, it has been isolated and characterized in a detergent micelle using the non-ionic detergent <i>n</i>-dodecyl-β-d-maltoside (DDM). We have now succeeded in isolating this complex without the use of detergents, using styrene-maleic acid (SMA) alternating copolymer. Intriguingly, a partially esterified copolymer formulation (SMA 1440, Cray Valley) was found to be most efficient in cyanobacterial thylakoid membranes. A host of biochemical, biophysical and functional assa"],"journal":["RSC advances"],"pubmed_title":["Non-detergent isolation of a cyanobacterial photosystem I using styrene maleic acid alternating copolymers."],"pmcid":["PMC9072662"],"funding_grant_id":["EPS-1004083","DGE-0801470","MCB-1452464","OCI-1053575"],"pubmed_authors":["Gumbart JC","Brady NG","Bruce BD","Ma Y","Li M"],"additional_accession":[]},"is_claimable":false,"name":"Non-detergent isolation of a cyanobacterial photosystem I using styrene maleic acid alternating copolymers.","description":"Photosystem I (PSI) from the thermophilic cyanobacterium <i>Thermosynechococcus elongatus</i> (Te) is the largest membrane protein complex to have had its structure solved by X-ray diffraction. This trimeric complex has 36 protein subunits, over 380 non-covalently bound cofactors and a molecular weight of ∼1.2 MDa. Previously, it has been isolated and characterized in a detergent micelle using the non-ionic detergent <i>n</i>-dodecyl-β-d-maltoside (DDM). We have now succeeded in isolating this complex without the use of detergents, using styrene-maleic acid (SMA) alternating copolymer. Intriguingly, a partially esterified copolymer formulation (SMA 1440, Cray Valley) was found to be most efficient in cyanobacterial thylakoid membranes. A host of biochemical, biophysical and functional assa","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2025-04-18T12:13:16.841Z","creation":"2025-04-06T21:51:51.095Z"},"accession":"S-EPMC9072662","cross_references":{"pubmed":["35527920"],"doi":["10.1039/c9ra04619d"]}}