SASBDB entries for UniProt ID:

SASDDY5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents

UniProt ID: P19491 (None-None) Glutamate receptor 2
Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.0 nm
Dmax 17.9 nm
VolumePorod 396 nm3

SASDDZ5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5

UniProt ID: P19491 (None-None) Glutamate receptor 2
Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.3 nm
Dmax 18.4 nm
VolumePorod 407 nm3

SASDD26 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 5.5

UniProt ID: P19491 (None-None) Glutamate receptor 2
Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 10 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 5.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.5 nm
Dmax 18.9 nm
VolumePorod 899 nm3

SASDD36 – AMPA subtype ionotropic Glutamate receptor GluA2 in the GYKI-53655 bound state, in stealth DDM detergents

UniProt ID: P19491 (None-None) Glutamate receptor 2
Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM GYKI-53655, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.3 nm
Dmax 18.6 nm
VolumePorod 384 nm3

SASDD66 – Phox homologue (PX) - C2 domains of human phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (PI3KC2α)

UniProt ID: O00443 (1405-1686) Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha experimental SAS data
DAMFILT model
Sample: Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha monomer, 33 kDa Homo sapiens protein
Buffer: 25 mM Tris 200 mM NaCl 5% Glycerol 0.5 mM TCEP, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 20
Molecular Basis for Membrane Recruitment by the PX and C2 Domains of Class II Phosphoinositide 3-Kinase-C2α. Structure (2018)
Chen KE, Tillu VA, Chandra M, Collins BM
RgGuinier 2.6 nm
Dmax 9.3 nm
VolumePorod 43 nm3

SASDD76 – Phox Homologue (PX) - C2 domains of human phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (PI3KC2α) in complex with inositol-hexaphosphate (IP6)

UniProt ID: O00443 (1405-1686) Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha experimental SAS data
DAMFILT model
Sample: Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha monomer, 33 kDa Homo sapiens protein
Buffer: 25 mM Tris 200 mM NaCl 5% Glycerol 0.5 mM TCEP 4 mM InsP6, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 20
Molecular Basis for Membrane Recruitment by the PX and C2 Domains of Class II Phosphoinositide 3-Kinase-C2α. Structure (2018)
Chen KE, Tillu VA, Chandra M, Collins BM
RgGuinier 2.6 nm
Dmax 9.3 nm
VolumePorod 48 nm3

SASDD86 – Full-length human NHLRC2 ( NHL repeat-containing protein 2 )

UniProt ID: Q8NBF2 (1-726) NHL repeat-containing protein 2
NHL repeat-containing protein 2 experimental SAS data
DAMFILT model
Sample: NHL repeat-containing protein 2 monomer, 80 kDa Homo sapiens protein
Buffer: 20 mM BisTris, 100 mM NaCl, 2 mM DTT, pH: 6.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jul 8
Structural analysis of human NHLRC2, mutations of which are associated with FINCA disease. PLoS One 13(8):e0202391 (2018)
Biterova E, Ignatyev A, Uusimaa J, Hinttala R, Ruddock LW
RgGuinier 3.6 nm
Dmax 14.7 nm
VolumePorod 121 nm3

SASDDB6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL)

UniProt ID: O43765 (1-313) Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length
Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length experimental SAS data
Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length Kratky plot
Sample: Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length dimer, 68 kDa Homo sapiens protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 5
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control. BMC Biol 16(1):76 (2018)
Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
RgGuinier 4.2 nm

SASDDC6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT)

UniProt ID: O43765 (1-213) Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains
Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains experimental SAS data
Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains Kratky plot
Sample: Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains dimer, 47 kDa Homo sapiens protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 5
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control. BMC Biol 16(1):76 (2018)
Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
RgGuinier 3.6 nm

SASDDD6 – Human Guanylate-binding protein (hGBP1)

UniProt ID: P32455 (None-None) Guanylate-binding protein 1
Guanylate-binding protein 1 experimental SAS data
DAMMIF model
Sample: Guanylate-binding protein 1 monomer, 68 kDa Homo sapiens protein
Buffer: 50 mM TRIS, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2018 Apr 30
Integrative dynamic structural biology unveils conformers essential for the oligomerization of a large GTPase. Elife 12 (2023)
Peulen TO, Hengstenberg CS, Biehl R, Dimura M, Lorenz C, Valeri A, Folz J, Hanke CA, Ince S, Vöpel T, Farago B, Gohlke H, Klare JP, Stadler AM, Seidel CAM, Herrmann C
RgGuinier 3.9 nm
Dmax 14.4 nm
VolumePorod 105 nm3