Browse by MODEL: Hybrid

SASDKG4 – Malus domestica double bond reductase (MdDBR) apoform

Malus domestica double bond reductase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Malus domestica double bond reductase dimer, 77 kDa Malus domestica protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl., pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2020 Oct 23
The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates International Journal of Biological Macromolecules 171:89-99 (2021)
Caliandro R, Polsinelli I, Demitri N, Musiani F, Martens S, Benini S
RgGuinier 3.0 nm
Dmax 9.9 nm
VolumePorod 110 nm3

SASDKH4 – Malus domestica double bond reductase in the presence of NADPH 5mM

Malus domestica double bond reductase experimental SAS data
PYMOL model
Sample: Malus domestica double bond reductase dimer, 77 kDa Malus domestica protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl, 5 mM NADPH, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2020 Oct 23
The structural and functional characterization of Malus domestica double bond reductase MdDBR provides insights towards the identification of its substrates International Journal of Biological Macromolecules 171:89-99 (2021)
Caliandro R, Polsinelli I, Demitri N, Musiani F, Martens S, Benini S
RgGuinier 3.1 nm
Dmax 10.7 nm
VolumePorod 99 nm3

SASDKK4 – A-type ATP synthase

n-Dodecyl-β-D-MaltopyranosideA-type ATP synthaseMonoclonal Antibody Fragment experimental SAS data
OTHER model
Sample: N-Dodecyl-β-D-Maltopyranoside, 77 kDa synthetic construct
A-type ATP synthase monomer, 655 kDa Thermus thermophilus protein
Monoclonal Antibody Fragment dimer, 33 kDa Homo sapiens protein
Buffer: 20 mM Tris/HCl, 100 mM sucrose, 100 mM NaCl, 2 mM MgCl2, 10% glycerol, 0.05% b-DDM, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2013 Mar 3
MPBuilder: A PyMOL Plugin for Building and Refinement of Solubilized Membrane Proteins Against Small Angle X-ray Scattering Data Journal of Molecular Biology :166888 (2021)
Molodenskiy D, Svergun D, Mertens H
RgGuinier 8.0 nm
Dmax 27.0 nm
VolumePorod 1549 nm3

SASDJV8 – Dimeric human ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358

Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358 experimental SAS data
CORAL model
Sample: Ganglioside-induced differentiation-associated protein 1, construct GDAP1∆303-358 dimer, 70 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Jun 28
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
Nguyen G, Sutinen A, Raasakka A, Muruganandam G, Loris R, Kursula P
RgGuinier 3.1 nm
Dmax 9.9 nm
VolumePorod 106 nm3

SASDJ39 – Monomeric human ganglioside-induced differentiation-associated protein 1-like 1, GDAP1L1

Ganglioside-induced differentiation-associated protein 1-like 1 (∆125-143 isoform) experimental SAS data
CORAL model
Sample: Ganglioside-induced differentiation-associated protein 1-like 1 (∆125-143 isoform) monomer, 44 kDa Homo sapiens protein
Buffer: 20 mM TRIS pH 7.5, 150 mM NaCl, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Dec 10
Structure of the Complete Dimeric Human GDAP1 Core Domain Provides Insights into Ligand Binding and Clustering of Disease Mutations Frontiers in Molecular Biosciences 7 (2021)
Nguyen G, Sutinen A, Raasakka A, Muruganandam G, Loris R, Kursula P
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 73 nm3

SASDKA4 – Complement factor P, properdin (FP) dimer

Properdin (dimer) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Properdin (dimer) dimer, 110 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 14
Properdin oligomers adopt rigid extended conformations supporting function. Elife 10 (2021)
Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR
RgGuinier 8.1 nm
Dmax 24.0 nm

SASDKB4 – Complement factor P, properdin (FP) trimer

Properdin (trimer) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Properdin (trimer) trimer, 165 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 14
Properdin oligomers adopt rigid extended conformations supporting function. Elife 10 (2021)
Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR
RgGuinier 10.2 nm
Dmax 27.0 nm

SASDKC4 – Complement factor P, properdin (FP) tetramer

Properdin (tetramer) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Properdin (tetramer) tetramer, 220 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Nov 14
Properdin oligomers adopt rigid extended conformations supporting function. Elife 10 (2021)
Pedersen DV, Pedersen MN, Mazarakis SM, Wang Y, Lindorff-Larsen K, Arleth L, Andersen GR
RgGuinier 13.1 nm
Dmax 36.0 nm

SASDJ35 – Glucose-6-phosphate dehydrogenase dimer

Glucose-6-phosphate 1-dehydrogenase experimental SAS data
PYMOL model
Sample: Glucose-6-phosphate 1-dehydrogenase dimer, 119 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2019 Jul 24
Long-range structural defects by pathogenic mutations in most severe glucose-6-phosphate dehydrogenase deficiency Proceedings of the National Academy of Sciences 118(4) (2021)
Horikoshi N, Hwang S, Gati C, Matsui T, Castillo-Orellana C, Raub A, Garcia A, Jabbarpour F, Batyuk A, Broweleit J, Xiang X, Chiang A, Broweleit R, Vöhringer-Martinez E, Mochly-Rosen D, Wakatsuki S
RgGuinier 3.6 nm
Dmax 12.1 nm
VolumePorod 160 nm3

SASDJ45 – Glucose-6-phosphate dehydrogenase P396L mutant

Glucose-6-phosphate 1-dehydrogenase P396L experimental SAS data
CORAL model
Sample: Glucose-6-phosphate 1-dehydrogenase P396L dimer, 119 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2019 Jul 24
Long-range structural defects by pathogenic mutations in most severe glucose-6-phosphate dehydrogenase deficiency Proceedings of the National Academy of Sciences 118(4) (2021)
Horikoshi N, Hwang S, Gati C, Matsui T, Castillo-Orellana C, Raub A, Garcia A, Jabbarpour F, Batyuk A, Broweleit J, Xiang X, Chiang A, Broweleit R, Vöhringer-Martinez E, Mochly-Rosen D, Wakatsuki S
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 178 nm3