| MWexperimental | 1514 | kDa |
| MWexpected | 878 | kDa |
| VPorod | 1703 | nm3 |
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log I(s)
1.54×100
1.54×10-1
1.54×10-2
1.54×10-3
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s, nm-1
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I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A, International Journal of Molecular Sciences 24(13):10720 (2023) DOISASDRW8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 450 mM NaCl
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplastic
ATP synthase gamma chain, chloroplastic
ATP synthase delta chain, chloroplastic
ATP synthase epsilon chain, chloroplastic
ATP synthase subunit a, chloroplastic
ATP synthase subunit b, chloroplastic
ATP synthase subunit b', chloroplastic
ATP synthase subunit c, chloroplastic
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
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Fits and models
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![ATP synthase subunit alpha, chloroplastic ATP synthase subunit beta, chloroplastic ATP synthase gamma chain, chloroplastic ATP synthase delta chain, chloroplastic ATP synthase epsilon chain, chloroplastic ATP synthase subunit a, chloroplastic ATP synthase subunit b, chloroplastic ATP synthase subunit b', chloroplastic ATP synthase subunit c, chloroplastic 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside OTHER [STATIC IMAGE] model](/media//pdb_file/SASDRW8_fit1_model1.png "Static model image")
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![ATP synthase subunit alpha, chloroplastic ATP synthase subunit beta, chloroplastic ATP synthase gamma chain, chloroplastic ATP synthase delta chain, chloroplastic ATP synthase epsilon chain, chloroplastic ATP synthase subunit a, chloroplastic ATP synthase subunit b, chloroplastic ATP synthase subunit b', chloroplastic ATP synthase subunit c, chloroplastic 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside OTHER [STATIC IMAGE] model](/media//pdb_file/SASDRW8_fit2_model1.png "Static model image")
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SAXS data from solutions of chloroplast FOF1-ATP synthase from Spinacia oleracea in 450 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH 8 were collected using a Rigaku MicroMax 007-HF instrument at the Moscow Institute of Physics and Technology (MIPT; Dolgoprudny, Russian Federation) equipped with a Multiwire gas-filled ASM DTR Triton 200 detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 20°C. One 5400 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The protein of study is a chloroplast FOF1-ATP synthase (cFOF1) from Spinacia oleracea solubilized in 0.04% (w/v) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside (tPCC-α-M). The values of the radii of gyration indicate dimers in which the distance between the monomers is ~ 200 Å. Thus, only two types of contacts are possible: FO/FO (presumably via c-ring) or F1/F1 (presumably via δ-subunit). An approximation of SAXS data with these models resulted in χ2 = 2.36 in the case of FO/FO dimers and χ2 = 1.20 for F1/F1 dimers with a fraction of dimeric cFOF1 96 ± 3 % and 68 ± 2 % for FO/FO and F1/F1 dimers. Thus, SAXS data confirm that cFOF1 purified by anion-exchange chromatography and incubated at 450 mM NaCl is a mixture of monomers and F1/F1 dimers with approximate volume fractions 32% and 68%. |
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