SASBDB entries for UniProt ID:

SASDRG8 – Astaxanthin-binding protein orange1 (AstaPo1) complexed with zeaxanthin

UniProt ID: S6BQ14 (21-223) Astaxanthin binding fasciclin family protein
Astaxanthin binding fasciclin family protein experimental SAS data
PYMOL model
Sample: Astaxanthin binding fasciclin family protein monomer, 22 kDa Coelastrella astaxanthina protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.6
Experiment: SAXS data collected at BM29, ESRF on 2021 Sep 24
Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaP. Commun Biol 6(1):471 (2023)
Kornilov FD, Slonimskiy YB, Lunegova DA, Egorkin NA, Savitskaya AG, Kleymenov SY, Maksimov EG, Goncharuk SA, Mineev KS, Sluchanko NN
RgGuinier 2.1 nm
Dmax 8.0 nm
VolumePorod 43 nm3

SASDRH8 – Astaxanthin-binding protein orange1 (AstaPo1) complexed with canthaxanthin

UniProt ID: S6BQ14 (21-223) Astaxanthin binding fasciclin family protein
Astaxanthin binding fasciclin family protein experimental SAS data
PYMOL model
Sample: Astaxanthin binding fasciclin family protein monomer, 22 kDa Coelastrella astaxanthina protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.6
Experiment: SAXS data collected at BM29, ESRF on 2021 Sep 24
Structural basis for the ligand promiscuity of the neofunctionalized, carotenoid-binding fasciclin domain protein AstaP. Commun Biol 6(1):471 (2023)
Kornilov FD, Slonimskiy YB, Lunegova DA, Egorkin NA, Savitskaya AG, Kleymenov SY, Maksimov EG, Goncharuk SA, Mineev KS, Sluchanko NN
RgGuinier 2.1 nm
Dmax 8.5 nm
VolumePorod 46 nm3

SASDRK8 – HOTag6 tetramerization domain followed by a (Pro-Ala)25 linker fused to human monoubiquitin

UniProt ID: None (None-None) HOTag-(PA)25-Ubiquitin
HOTag-(PA)25-Ubiquitin experimental SAS data
HOTag-(PA)25-Ubiquitin Kratky plot
Sample: HOTag-(PA)25-Ubiquitin tetramer, 68 kDa synthetic construct protein
Buffer: 20 mM sodium phosphate, 0.5 mM EDTA, 0.02 % NaN3, pH: 6.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2023 Mar 22
Polyubiquitin ligand-induced phase transitions are optimized by spacing between ubiquitin units Proceedings of the National Academy of Sciences 120(42) (2023)
Galagedera S, Dao T, Enos S, Chaudhuri A, Schmit J, Castañeda C
RgGuinier 6.3 nm
Dmax 24.9 nm
VolumePorod 180 nm3

SASDRL8 – Bovine serum albumin

UniProt ID: P02769 (25-607) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 66 kDa Bos taurus protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2022 Jun 7
NSRRC TPS13A standard protein archive
Orion Shih
RgGuinier 2.9 nm
Dmax 8.9 nm
VolumePorod 84 nm3

SASDRM8 – Lysozyme C (Gallus gallus)

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
Lysozyme C Kratky plot
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM sodium acetate, 50 mM NaCl, pH: 4
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2021 Apr 2
NSRRC TPS13A standard protein archive
Orion Shih
RgGuinier 1.4 nm
Dmax 4.6 nm
VolumePorod 13 nm3

SASDRN8 – α/β Hemoglobin (human)

UniProt ID: P69905 (1-142) Hemoglobin subunit alpha

UniProt ID: P68871 (1-147) Hemoglobin subunit beta
Hemoglobin subunit alphaHemoglobin subunit beta experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Kratky plot
Sample: Hemoglobin subunit alpha dimer, 31 kDa Homo sapiens protein
Hemoglobin subunit beta dimer, 32 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2021 Oct 7
NSRRC TPS13A standard protein archive
Orion Shih
RgGuinier 2.5 nm
Dmax 9.2 nm
VolumePorod 97 nm3

SASDRQ8 – Bovine serum albumin monomer separated using asymmetric flow field flow fractionation (AFFFF)

UniProt ID: P02769 (25-607) Albumin
Albumin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Albumin monomer, 66 kDa Bos taurus protein
Buffer: 10 mM HEPES, 5 mM NaCl, 0.1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Jun 8
Quantitative size-resolved characterization of mRNA nanoparticles by in-line coupling of asymmetrical-flow field-flow fractionation with small angle X-ray scattering. Sci Rep 13(1):15764 (2023)
Graewert MA, Wilhelmy C, Bacic T, Schumacher J, Blanchet C, Meier F, Drexel R, Welz R, Kolb B, Bartels K, Nawroth T, Klein T, Svergun D, Langguth P, Haas H
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 104 nm3

SASDRR8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea purified by anion-exchange chromatography (~ 300 mM NaCl)

UniProt ID: P06450 (1-507) ATP synthase subunit alpha, chloroplastic

UniProt ID: P00825 (1-498) ATP synthase subunit beta, chloroplastic

UniProt ID: P05435 (1-364) ATP synthase gamma chain, chloroplastic

UniProt ID: P11402 (1-257) ATP synthase delta chain, chloroplastic

UniProt ID: P00833 (1-134) ATP synthase epsilon chain, chloroplastic

UniProt ID: P06451 (1-247) ATP synthase subunit a, chloroplastic

UniProt ID: P06453 (1-184) ATP synthase subunit b, chloroplastic

UniProt ID: P31853 (1-222) ATP synthase subunit b', chloroplastic

UniProt ID: P69447 (1-81) ATP synthase subunit c, chloroplastic

UniProt ID: None (None-None) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
MEMPROT model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 300 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
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
RgGuinier 6.6 nm
Dmax 27.5 nm
VolumePorod 927 nm3

SASDRS8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 150 mM NaCl

UniProt ID: P06450 (1-507) ATP synthase subunit alpha, chloroplastic

UniProt ID: P00825 (1-498) ATP synthase subunit beta, chloroplastic

UniProt ID: P05435 (1-364) ATP synthase gamma chain, chloroplastic

UniProt ID: P11402 (1-257) ATP synthase delta chain, chloroplastic

UniProt ID: P00833 (1-134) ATP synthase epsilon chain, chloroplastic

UniProt ID: P06451 (1-247) ATP synthase subunit a, chloroplastic

UniProt ID: P06453 (1-184) ATP synthase subunit b, chloroplastic

UniProt ID: P31853 (1-222) ATP synthase subunit b', chloroplastic

UniProt ID: P69447 (1-81) ATP synthase subunit c, chloroplastic

UniProt ID: None (None-None) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 150 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
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
RgGuinier 9.6 nm
Dmax 41.5 nm
VolumePorod 1506 nm3

SASDRT8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea at 250 mM NaCl

UniProt ID: P06450 (1-507) ATP synthase subunit alpha, chloroplastic

UniProt ID: P00825 (1-498) ATP synthase subunit beta, chloroplastic

UniProt ID: P05435 (1-364) ATP synthase gamma chain, chloroplastic

UniProt ID: P11402 (1-257) ATP synthase delta chain, chloroplastic

UniProt ID: P00833 (1-134) ATP synthase epsilon chain, chloroplastic

UniProt ID: P06451 (1-247) ATP synthase subunit a, chloroplastic

UniProt ID: P06453 (1-184) ATP synthase subunit b, chloroplastic

UniProt ID: P31853 (1-222) ATP synthase subunit b', chloroplastic

UniProt ID: P69447 (1-81) ATP synthase subunit c, chloroplastic

UniProt ID: None (None-None) 4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside
ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
OTHER [STATIC IMAGE] model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 250 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
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
RgGuinier 7.4 nm
Dmax 33.0 nm
VolumePorod 949 nm3