SASBDB entries for UniProt ID:

SASDSC2 – Sulfite reductase truncated linker (ΔAAPSQS) flavoprotein reduced with 10 molar equivalents sodium dithionite

UniProt ID: P38038 (1-599) Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217)
Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) experimental SAS data
Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) Kratky plot
Sample: Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) octamer, 526 kDa Escherichia coli (strain … protein
Buffer: 50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment: SANS data collected at EQ-SANS, Spallation Neutron Source on 2022 Jul 15
Domain crossover in the reductase subunit of NADPH-dependent assimilatory sulfite reductase. J Struct Biol 215(4):108028 (2023)
Walia N, Murray DT, Garg Y, He H, Weiss KL, Nagy G, Elizabeth Stroupe M
RgGuinier 7.6 nm
Dmax 25.0 nm
VolumePorod 952 nm3

SASDSD2 – Recombinant Heavy-chain-only nanobody C5-Fc (glycosylated)

UniProt ID: None (None-None) Immunoglobulin heavy constant gamma 1
Immunoglobulin heavy constant gamma 1 experimental SAS data
PYMOL model
Sample: Immunoglobulin heavy constant gamma 1 monomer, 78 kDa Homo sapiens protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.6 mM KCl buffer, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Sep 28
The solution structure of the heavy chain-only C5-Fc nanobody reveals exposed variable regions that are optimal for COVID-19 antigen interactions. J Biol Chem :105337 (2023)
Gao X, Thrush JW, Gor J, Naismith JH, Owens RJ, Perkins SJ
RgGuinier 3.9 nm
Dmax 13.2 nm
VolumePorod 157 nm3

SASDSE2 – Recombinant Heavy-chain-only nanobody C5-Fc (Deglycosylated)

UniProt ID: None (None-None) Immunoglobulin heavy constant gamma 1
Immunoglobulin heavy constant gamma 1 experimental SAS data
PYMOL model
Sample: Immunoglobulin heavy constant gamma 1 monomer, 78 kDa Homo sapiens protein
Buffer: 20 mM L-histidine, 138 mM NaCl, 2.6 mM KCl buffer, pH: 6
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Sep 28
The solution structure of the heavy chain-only C5-Fc nanobody reveals exposed variable regions that are optimal for COVID-19 antigen interactions. J Biol Chem :105337 (2023)
Gao X, Thrush JW, Gor J, Naismith JH, Owens RJ, Perkins SJ
RgGuinier 4.0 nm
Dmax 13.1 nm
VolumePorod 175 nm3

SASDSF2 – K48-linked diubiquitin

UniProt ID: P0CG48 (1-152) Polyubiquitin-C
Polyubiquitin-C experimental SAS data
OTHER model
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin. Dalton Trans (2023)
Mangini V, Grasso G, Belviso BD, Sciacca MFM, Lanza V, Caliandro R, Milardi D
RgGuinier 1.9 nm
Dmax 6.5 nm
VolumePorod 22 nm3

SASDSG2 – K48-linked diubiquitin in the presence of zinc ion

UniProt ID: P0CG48 (1-152) Polyubiquitin-C
Polyubiquitin-C experimental SAS data
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin. Dalton Trans (2023)
Mangini V, Grasso G, Belviso BD, Sciacca MFM, Lanza V, Caliandro R, Milardi D
RgGuinier 2.0 nm
Dmax 7.5 nm
VolumePorod 20 nm3

SASDSH2 – K48-linked diubiquitin in the presence of copper (II) ion

UniProt ID: P0CG48 (1-152) Polyubiquitin-C
Polyubiquitin-C experimental SAS data
Sample: Polyubiquitin-C monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Feb 1
Stretching the chains: the destabilizing impact of Cu(2+) and Zn(2+) ions on K48-linked diubiquitin. Dalton Trans (2023)
Mangini V, Grasso G, Belviso BD, Sciacca MFM, Lanza V, Caliandro R, Milardi D
RgGuinier 1.9 nm
Dmax 6.3 nm
VolumePorod 20 nm3

SASDSJ2 – Ribosome maturation factor RimP bound to 30S ribosomal protein S12 (RimP-uS12 complex from Staphylococcus aureus)

UniProt ID: Q5HGG6 (2-155) Ribosome maturation factor RimP

UniProt ID: Q5HID0 (2-136) 30S ribosomal protein S12
Ribosome maturation factor RimP30S ribosomal protein S12 experimental SAS data
DAMMIN model
Sample: Ribosome maturation factor RimP monomer, 18 kDa Staphylococcus aureus (strain … protein
30S ribosomal protein S12 monomer, 15 kDa Staphylococcus aureus (strain … protein
Buffer: 50 mM sodium phosphate, 200 mM NaCl, pH: 7
Experiment: SAXS data collected at Xeuss 3.0 SAXS/WAXS System, JINR on 2023 Feb 16
Structural aspects of RimP binding on small ribosomal subunit from Staphylococcus aureus. Structure (2023)
Garaeva N, Fatkhullin B, Murzakhanov F, Gafurov M, Golubev A, Bikmullin A, Glazyrin M, Kieffer B, Jenner L, Klochkov V, Aganov A, Rogachev A, Ivankov O, Validov S, Yusupov M, Usachev K
RgGuinier 2.4 nm
Dmax 10.0 nm
VolumePorod 39 nm3

SASDSK2 – SEC-SAXS data of wild-type estrogen receptor alpha, N-terminal domain (NTD) at pH 7.4

UniProt ID: P03372 (1-184) Estrogen receptor
Estrogen receptor experimental SAS data
Estrogen receptor Kratky plot
Sample: Estrogen receptor monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 150 mM NaCl, 0.5 mM EDTA, 0.1 mM PMSF, pH: 7.4
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 21
The sequence–structure–function relationship of intrinsic ERα disorder Nature (2025)
Du Z, Wang H, Luo S, Yun Z, Wu C, Yang W, Buck M, Zheng W, Hansen A, Kao H, Yang S
RgGuinier 3.2 nm
Dmax 14.0 nm
VolumePorod 47 nm3

SASDSL2 – Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (EMAPII) at pH 8

UniProt ID: Q12904 (147-312) Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 experimental SAS data
Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (EMAPII) at pH 8 Rg histogram
Sample: Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 monomer, 20 kDa Homo sapiens protein
Buffer: 50 mM Tris, 150 mM NaCl, 1mM DTT, pH: 8
Experiment: SAXS data collected at Xenocs Xeuss 2.0 with MetalJet, Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University on 2022 Oct 12
Solution structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex
Michal Taube
RgGuinier 1.9 nm
Dmax 7.7 nm
VolumePorod 27 nm3

SASDSM2 – AtCP12-2 in an oxidized form

UniProt ID: A0A178VHQ2 (54-131) CP12-2 (D77G)
CP12-2 (D77G) experimental SAS data
AtCP12-2 in an oxidized form Rg histogram
Sample: CP12-2 (D77G) monomer, 8 kDa Arabidopsis thaliana protein
Buffer: 25 mM potassium phosphate, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 15
Conformational Disorder Analysis of the Conditionally Disordered Protein CP12 from Arabidopsis thaliana in Its Different Redox States International Journal of Molecular Sciences 24(11):9308 (2023)
Del Giudice A, Gurrieri L, Galantini L, Fanti S, Trost P, Sparla F, Fermani S
RgGuinier 2.0 nm
Dmax 9.0 nm
VolumePorod 10 nm3