Browse by MODEL: Ab initio only

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

SASDMJ5 – Four-component synthetic liposomes composed of 20% bPS + 13.3% POPC + 33.3% SM + 33.3% Chol lipid mixtures loaded with M1 protein

Four-component synthetic liposomes composed of 20% bPS + 13.3% POPC + 33.3% SM + 33.3% 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 20% bPS + 13.3% POPC + 33.3% SM + 33.3% 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

SASDMK5 – Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein.

Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein. (lipid:M1 molar ration 4:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Native liposomes composed of lipids extracted from A/Puerto Rico/8/34 (H1N1) virus envelope loaded with M1 protein. (lipid:M1 molar ration 4:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 26
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

SASDML5 – Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein

Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein (lipid:M1 molar ration 4:1) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Proteoliposomes composed of lipids from A/Puerto Rico/8/34 (H1N1) virus envelope together with the HA LI45 peptides loaded with M1 protein (lipid:M1 molar ration 4:1) monomer, 2000 kDa
Buffer: 100 mM NaCl, 50 mM MES buffer, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Nov 26
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

SASDJ44 – Human Complex I assembly factor ACAD9 complexed with ECSIT

Complex I assembly factor ACAD9, mitochondrialEvolutionarily conserved signaling intermediate in Toll pathway, mitochondrial experimental SAS data
DAMFILT model
Sample: Complex I assembly factor ACAD9, mitochondrial dimer, 130 kDa Homo sapiens protein
Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial dimer, 93 kDa Homo sapiens protein
Buffer: 25mM Tris-HCl, 150mM NaCl, 0.1mM DTT, and 5% glycerol, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Nov 2
Molecular mechanism of interactions between ACAD9 and binding partners in mitochondrial respiratory complex I assembly iScience 24(10):103153 (2021)
Xia C, Lou B, Fu Z, Mohsen A, Shen A, Vockley J, Kim J
RgGuinier 5.1 nm
Dmax 16.8 nm
VolumePorod 514 nm3

SASDJ54 – Human Complex I assembly factor ACAD9 complexed with ECSIT and SMT3-NDUFAF1

Complex I assembly factor ACAD9, mitochondrialEvolutionarily conserved signaling intermediate in Toll pathway, mitochondrialComplex I intermediate-associated protein 30, mitochondrial experimental SAS data
DAMMIF model
Sample: Complex I assembly factor ACAD9, mitochondrial tetramer, 259 kDa Homo sapiens protein
Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial tetramer, 184 kDa Homo sapiens protein
Complex I intermediate-associated protein 30, mitochondrial tetramer, 190 kDa Homo sapiens protein
Buffer: 25mM Tris-HCl, 150mM NaCl, 0.1mM DTT, and 5% glycerol, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2017 Nov 2
Molecular mechanism of interactions between ACAD9 and binding partners in mitochondrial respiratory complex I assembly iScience 24(10):103153 (2021)
Xia C, Lou B, Fu Z, Mohsen A, Shen A, Vockley J, Kim J
RgGuinier 6.6 nm
Dmax 21.6 nm
VolumePorod 1340 nm3