Browse by MODEL: Ab initio only

SASDNB3 – Homodimerisation of the CP110 C-terminus coiled-coil domain

Centriolar coiled-coil protein of 110 kDa experimental SAS data
DAMMIF model
Sample: Centriolar coiled-coil protein of 110 kDa dimer, 20 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH 7.5, 100 mM NaCl, 1 mM DTT, 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Feb 23
Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends. J Cell Biol 224(3) (2025)
Iyer SS, Chen F, Ogunmolu FE, Moradi S, Volkov VA, van Grinsven EJ, van Hoorn C, Wu J, Andrea N, Hua S, Jiang K, Vakonakis I, Potočnjak M, Herzog F, Gigant B, Gudimchuk N, Stecker KE, Dogterom M, Steinmetz MO, Akhmanova A
RgGuinier 3.5 nm
Dmax 12.5 nm
VolumePorod 33 nm3

SASDMK7 – HomA outer membrane protein

HomA outer membrane protein experimental SAS data
DAMMIN model
Sample: HomA outer membrane protein dimer, 146 kDa Helicobacter pylori protein
Buffer: 20 mM Tris-Cl, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BL-18, INDUS-2 on 2021 Feb 2
Biophysical characterization of the homodimers of HomA and HomB, outer membrane proteins of Helicobacter pylori. Sci Rep 11(1):24471 (2021)
Tamrakar A, Singh R, Kumar A, Makde RD, Ashish, Kodgire P
RgGuinier 8.3 nm
Dmax 28.2 nm
VolumePorod 426 nm3

SASDML7 – HomB outer membrane protein

HomB outer membrane protein experimental SAS data
DAMMIN model
Sample: HomB outer membrane protein dimer, 148 kDa Helicobacter pylori protein
Buffer: 20 mM Tris-Cl, 200 mM NaCl, 5 mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BL-18, INDUS-2 on 2021 Feb 2
Biophysical characterization of the homodimers of HomA and HomB, outer membrane proteins of Helicobacter pylori. Sci Rep 11(1):24471 (2021)
Tamrakar A, Singh R, Kumar A, Makde RD, Ashish, Kodgire P
RgGuinier 8.2 nm
Dmax 27.1 nm
VolumePorod 500 nm3

SASDMR6 – 5-10-5 gapmer phosphorothioate antisense oligonucleotide

5-10-5 gapmer phosphorothioate antisense oligonucleotide experimental SAS data
DAMFILT model
Sample: 5-10-5 gapmer phosphorothioate antisense oligonucleotide dimer, 14 kDa
Buffer: 20 mM Tris-Cl (pH 7.5), 250 mM KCl, 50 mM L-proline, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28
Structural basis of dimerization and nucleic acid binding of human DBHS proteins NONO and PSPC1. Nucleic Acids Res (2021)
Knott GJ, Chong YS, Passon DM, Liang XH, Deplazes E, Conte MR, Marshall AC, Lee M, Fox AH, Bond CS
RgGuinier 1.8 nm
Dmax 8.5 nm
VolumePorod 15 nm3

SASDJ89 – Sensory rhodopsin II - transducer complex (NpSRII/NpHtrII) in detergent at 1400 mM NaCl studied with SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
GASBOR model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 1400 mM NaCl, 49.4 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Feb 10
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 8.6 nm
Dmax 39.0 nm

SASDJ99 – Sensory rhodopsin II - transducer complex (NpSRII/NpHtrII) in detergent at 2800 mM NaCl studied with SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
GASBOR model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 2800 mM NaCl, 76.6 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Feb 10
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 9.0 nm
Dmax 39.0 nm

SASDJA9 – Sensory rhodopsin II - transducer complex (NpSRII/NpHtrII) in detergent at 4000 mM NaCl studied with SANS

Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
GASBOR model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 4000 mM NaCl, 100 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Jan 25
Ambiguities in and completeness of SAS data analysis of membrane proteins: the case of the sensory rhodopsin II–transducer complex Acta Crystallographica Section D Structural Biology 77(11) (2021)
Ryzhykau Y, Vlasov A, Orekhov P, Rulev M, Rogachev A, Vlasova A, Kazantsev A, Verteletskiy D, Skoi V, Brennich M, Pernot P, Murugova T, Gordeliy V, Kuklin A
RgGuinier 10.4 nm
Dmax 39.0 nm

SASDMF5 – Two-component synthetic liposomes composed of 10% DOPS + 90% DOPC lipid mixtures loaded with M1 protein

Two-component synthetic liposomes composed of 10% DOPS + 90% DOPC lipid mixtures loaded with M1 protein ((lipid:M1 molar ratio 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Two-component synthetic liposomes composed of 10% DOPS + 90% DOPC lipid mixtures loaded with M1 protein ((lipid:M1 molar ratio 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 30
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
Kordyukova L, Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDMG5 – Two-component synthetic liposomes composed of 30% DOPS + 70% DOPC lipid mixtures loaded with M1 protein

Two-component synthetic liposomes composed of 30% DOPS + 70% DOPC lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Two-component synthetic liposomes composed of 30% DOPS + 70% DOPC lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 31
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
Kordyukova L, Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O

SASDMH5 – Four-component synthetic liposomes composed of 30% bPS + 10% POPC + 40% SM + 20% Chol lipid mixtures loaded with M1 protein

Four-component synthetic liposomes composed of 30% bPS + 10% POPC + 40% SM + 20% Chol lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Four-component synthetic liposomes composed of 30% bPS + 10% POPC + 40% SM + 20% Chol lipid mixtures loaded with M1 protein (lipid:M1 molar ration 20:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 31
The Cytoplasmic Tail of Influenza A Virus Hemagglutinin and Membrane Lipid Composition Change the Mode of M1 Protein Association with the Lipid Bilayer Membranes 11(10):772 (2021)
Kordyukova L, Konarev P, Fedorova N, Shtykova E, Ksenofontov A, Loshkarev N, Dadinova L, Timofeeva T, Abramchuk S, Moiseenko A, Baratova L, Svergun D, Batishchev O