SASBDB entries for UniProt ID:

SASDTU4 – 24×FerSUMO - Chimeric protein complex of ferritin from Helicobacter pylori fused to an N-terminal His6-SUMO protein tag

UniProt ID: Q9ZLI1 (5-167) Bacterial non-heme ferritin (N19Q, I59V, N-terminal His-SUMO fusion)
Bacterial non-heme ferritin (N19Q, I59V, N-terminal His-SUMO fusion) experimental SAS data
CORAL model
Sample: Bacterial non-heme ferritin (N19Q, I59V, N-terminal His-SUMO fusion) 24-mer, 755 kDa Helicobacter pylori (strain … protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2022 Jul 30
Ferritin-based fusion protein shows octameric deadlock state of self-assembly Biochemical and Biophysical Research Communications 690:149276 (2024)
Sudarev V, Gette M, Bazhenov S, Tilinova O, Zinovev E, Manukhov I, Kuklin A, Ryzhykau Y, Vlasov A
RgGuinier 7.6 nm
Dmax 25.0 nm
VolumePorod 2010 nm3

SASDTV4 – 8×FerSUMO - Chimeric protein complex of ferritin from Helicobacter pylori fused to an N-terminal His6-SUMO protein tag

UniProt ID: Q9ZLI1 (5-167) Bacterial non-heme ferritin (N19Q, I59V, N-terminal His-SUMO fusion)
Bacterial non-heme ferritin (N19Q, I59V, N-terminal His-SUMO fusion) experimental SAS data
PHYRE2 model
Sample: Bacterial non-heme ferritin (N19Q, I59V, N-terminal His-SUMO fusion) octamer, 252 kDa Helicobacter pylori (strain … protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2022 Jul 17
Ferritin-based fusion protein shows octameric deadlock state of self-assembly Biochemical and Biophysical Research Communications 690:149276 (2024)
Sudarev V, Gette M, Bazhenov S, Tilinova O, Zinovev E, Manukhov I, Kuklin A, Ryzhykau Y, Vlasov A
RgGuinier 5.4 nm
Dmax 16.0 nm
VolumePorod 618 nm3

SASDTW4 – Ferritin from Helicobacter pylori with an N-terminal His6-tag

UniProt ID: Q9ZLI1 (5-167) Bacterial non-heme ferritin (N19Q, I59V)
Bacterial non-heme ferritin (N19Q, I59V) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bacterial non-heme ferritin (N19Q, I59V) 24-mer, 480 kDa Helicobacter pylori (strain … protein
Buffer: 20 mM Tris, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2022 Dec 14
Ferritin-based fusion protein shows octameric deadlock state of self-assembly Biochemical and Biophysical Research Communications 690:149276 (2024)
Sudarev V, Gette M, Bazhenov S, Tilinova O, Zinovev E, Manukhov I, Kuklin A, Ryzhykau Y, Vlasov A
RgGuinier 5.6 nm
Dmax 14.5 nm
VolumePorod 674 nm3

SASDTX4 – G-actin - Skeletal muscle actin from Oryctolagus cuniculus: globular actin monomers

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris/Tris-HCl, 0.1 mM CaCl2, 1 mM NaN3, 0.2 mM ATP, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 1
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 2.9 nm
Dmax 8.5 nm
VolumePorod 58 nm3

SASDTY4 – F-actin - Skeletal muscle actin from Oryctolagus cuniculus: fibrillar actin

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
DAMMIF model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris/Tris-HCl, 0.1 mM CaCl2, 1 mM NaN3, 1.0 mM ATP, 50 mM KCl, 2 mM MgCl2, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 1
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 15.7 nm
Dmax 60.0 nm
VolumePorod 4710 nm3

SASDTZ4 – I-actin - Skeletal muscle actin from Oryctolagus cuniculus: oligomer of time-inactivated actin (peak SEC fraction)

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris/Tris-HCl, 2.0 mM EDTA, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Nov 16
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 4.9 nm
Dmax 22.0 nm
VolumePorod 549 nm3

SASDT25 – G- / I-actin mixture - Skeletal muscle actin from Oryctolagus cuniculus: mixture of globular actin monomers and inactivated actin monomers and dimers

UniProt ID: P68135 (1-377) Actin, alpha skeletal muscle
Actin, alpha skeletal muscle experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Actin, alpha skeletal muscle monomer, 42 kDa Oryctolagus cuniculus protein
Buffer: 5 mM Tris, 0.1 mM CaCl2, 1 mM NaN3, 0.2 mM ATP, pH: 8.1
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2021 Jul 5
Small-angle X-ray scattering structural insights into alternative pathway of actin oligomerization associated with inactivated state Biochemical and Biophysical Research Communications :149340 (2023)
Ryzhykau Y, Povarova O, Dronova E, Kuklina D, Antifeeva I, Ilyinsky N, Okhrimenko I, Semenov Y, Kuklin A, Ivanovich V, Fonin A, Uversky V, Turoverov K, Kuznetsova I
RgGuinier 3.1 nm
Dmax 12.0 nm
VolumePorod 84 nm3

SASDT35 – N-cadherin extracellular domains EC1-EC5

UniProt ID: P15116 (160-714) Cadherin-2
Cadherin-2 experimental SAS data
Cadherin-2 Kratky plot
Sample: Cadherin-2 dimer, 123 kDa Mus musculus protein
Buffer: 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 1
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell 187(5):1296-1311.e26 (2024)
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
RgGuinier 8.8 nm
Dmax 40.0 nm
VolumePorod 496 nm3

SASDT45 – N-cadherin extracellular domains EC4-EC5

UniProt ID: P15116 (490-702) Cadherin-2
Cadherin-2 experimental SAS data
Cadherin-2 Kratky plot
Sample: Cadherin-2 monomer, 24 kDa Mus musculus protein
Buffer: 20 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 7.5
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 1
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell 187(5):1296-1311.e26 (2024)
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
RgGuinier 3.4 nm
Dmax 12.6 nm
VolumePorod 63 nm3

SASDTC5 – Full-length E3 ubiquitin-protein ligase HACE1

UniProt ID: Q8IYU2 (1-909) E3 ubiquitin-protein ligase HACE1
E3 ubiquitin-protein ligase HACE1 experimental SAS data
GASBOR model
Sample: E3 ubiquitin-protein ligase HACE1 dimer, 205 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 50 mM NaCl, 5 mM DTT, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Apr 21
Structural mechanisms of autoinhibition and substrate recognition by the ubiquitin ligase HACE1 Nature Structural & Molecular Biology (2024)
Düring J, Wolter M, Toplak J, Torres C, Dybkov O, Fokkens T, Bohnsack K, Urlaub H, Steinchen W, Dienemann C, Lorenz S
RgGuinier 5.2 nm
Dmax 16.4 nm
VolumePorod 379 nm3