Browse by ORGANISM: Homo sapiens (Human)

SASDDC3 – Human mitochondrial cysteine desulfurase-ISCU (NFS1, ISD11, Acp and ISCU heterodimer complex)

Cysteine desulfurase, mitochondrialLYR motif-containing protein 4Acyl carrier proteinIron-sulfur cluster assembly enzyme ISCU, mitochondrial experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cysteine desulfurase, mitochondrial dimer, 90 kDa Homo sapiens protein
LYR motif-containing protein 4 dimer, 23 kDa Homo sapiens protein
Acyl carrier protein dimer, 22 kDa Escherichia coli protein
Iron-sulfur cluster assembly enzyme ISCU, mitochondrial dimer, 29 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, NMRFAM on 2017 May 22
Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering. Structure 26(8):1127-1136.e4 (2018)
Cai K, Frederick RO, Dashti H, Markley JL
RgGuinier 3.9 nm
Dmax 13.7 nm
VolumePorod 218 nm3

SASDDD3 – Human mitochondrial cysteine desulfurase-ISCU-Frataxin (NFS1, ISD11 and Acp heterodimer complex)

Cysteine desulfurase, mitochondrialLYR motif-containing protein 4Acyl carrier proteinIron-sulfur cluster assembly enzyme ISCU, mitochondrialFrataxin, mitochondrial experimental SAS data
HADDOCK model
Sample: Cysteine desulfurase, mitochondrial dimer, 90 kDa Homo sapiens protein
LYR motif-containing protein 4 dimer, 23 kDa Homo sapiens protein
Acyl carrier protein dimer, 22 kDa Escherichia coli protein
Iron-sulfur cluster assembly enzyme ISCU, mitochondrial dimer, 29 kDa Homo sapiens protein
Frataxin, mitochondrial dimer, 29 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, NMRFAM on 2017 Apr 18
Architectural Features of Human Mitochondrial Cysteine Desulfurase Complexes from Crosslinking Mass Spectrometry and Small-Angle X-Ray Scattering. Structure 26(8):1127-1136.e4 (2018)
Cai K, Frederick RO, Dashti H, Markley JL
RgGuinier 4.1 nm
Dmax 14.4 nm
VolumePorod 287 nm3

SASDDJ9 – Conformation of the R1-3 human dystrophin fragment (SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 4.2 nm
Dmax 17.7 nm
VolumePorod 46 nm3

SASDDK9 – Conformation of R1-3 human dystrophin fragment in interaction with zwitterionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment experimental SAS data
DAMMIF model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 4.1 nm
Dmax 17.8 nm
VolumePorod 50 nm3

SASDDL9 – Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment experimental SAS data
YASARA model
Sample: R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer: 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7
Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF
RgGuinier 6.2 nm
Dmax 24.8 nm
VolumePorod 100 nm3

SASDDP6 – Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment (6G08 F(ab))

Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment experimental SAS data
Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment Kratky plot
Sample: Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment monomer, 46 kDa Homo sapiens protein
Buffer: 50mM HEPES, 150mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 5
Evaluating Anti-CD32b F(ab) Conformation Using Molecular Dynamics and Small-Angle X-Ray Scattering. Biophys J 115(2):289-299 (2018)
Sutton EJ, Bradshaw RT, Orr CM, Frendéus B, Larsson G, Teige I, Cragg MS, Tews I, Essex JW
RgGuinier 2.6 nm
Dmax 7.3 nm
VolumePorod 68 nm3

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

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)

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

SASDCR9 – Kif2A-tubulin-DARP complex in the presence of AMP-PNP

Designed Ankyrin Repeat Protein D1Kinesin-like protein KIF2ATubulin alpha-1B chainTubulin beta-2B chain experimental SAS data
DAMMIF model
Sample: Designed Ankyrin Repeat Protein D1 monomer, 18 kDa synthetic construct protein
Kinesin-like protein KIF2A monomer, 48 kDa Homo sapiens protein
Tubulin alpha-1B chain dimer, 100 kDa Bos taurus protein
Tubulin beta-2B chain dimer, 100 kDa Bos taurus protein
Buffer: HEPES 20 mM, MgCl2 1mM, NaCl 150mM, pH: 7.2
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 16
Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate. Nat Commun 9(1):2628 (2018)
Trofimova D, Paydar M, Zara A, Talje L, Kwok BH, Allingham JS
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 374 nm3

SASDDT4 – Fc region of Immunoglobulin G1 (IgG1 Fc)

Immunoglobulin heavy constant gamma 1 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 dimer, 53 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 70 nm3