Browse by MODEL: Ab initio only

SASDMY8 – Iron oxide nanoparticles (NP-N3) (60% of 9 kDa PEG tails)

Iron oxide nanoparticles (NP-N3) (60% of 9 kDa PEG tails) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Iron oxide nanoparticles (NP-N3) (60% of 9 kDa PEG tails) 0, 5000 kDa
Buffer: 0.05 M Tris-HCl, 0.05 M NaCl, 0.01 M KCl, 0.005 M MgCl2, pH: 4.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 23
Coat Protein-Dependent Behavior of Poly(ethylene glycol) Tails in Iron Oxide Core Virus-like Nanoparticles. ACS Appl Mater Interfaces 7(22):12089-98 (2015)
Malyutin AG, Cheng H, Sanchez-Felix OR, Carlson K, Stein BD, Konarev PV, Svergun DI, Dragnea B, Bronstein LM
Dmax 26.0 nm

SASDMZ8 – Iron oxide nanoparticles (NP-P3) (60% of 5 kDa PEG tails)

Iron oxide nanoparticles (NP-P3) (60% of 5 kDa PEG tails) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Iron oxide nanoparticles (NP-P3) (60% of 5 kDa PEG tails) 0, 5000 kDa
Buffer: 0.05 M Tris-HCl, 0.05 M NaCl, 0.01 M KCl, 0.005 M MgCl2, pH: 4.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 23
Coat Protein-Dependent Behavior of Poly(ethylene glycol) Tails in Iron Oxide Core Virus-like Nanoparticles. ACS Appl Mater Interfaces 7(22):12089-98 (2015)
Malyutin AG, Cheng H, Sanchez-Felix OR, Carlson K, Stein BD, Konarev PV, Svergun DI, Dragnea B, Bronstein LM
Dmax 26.0 nm

SASDM29 – Iron oxide nanoparticles (NP-N2) encapsulated into brome mosaic virus (BMV)

Iron oxide nanoparticles (NP-N2) encapsulated into brome mosaic virus (BMV) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Iron oxide nanoparticles (NP-N2) encapsulated into brome mosaic virus (BMV) 0, 5000 kDa
Buffer: 0.05 M Tris-HCl, 0.05 M NaCl, 0.01 M KCl, 0.005 M MgCl2, pH: 4.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 23
Coat Protein-Dependent Behavior of Poly(ethylene glycol) Tails in Iron Oxide Core Virus-like Nanoparticles. ACS Appl Mater Interfaces 7(22):12089-98 (2015)
Malyutin AG, Cheng H, Sanchez-Felix OR, Carlson K, Stein BD, Konarev PV, Svergun DI, Dragnea B, Bronstein LM
Dmax 25.5 nm

SASDM39 – Iron oxide nanoparticles (NP-P3) encapsulated into brome mosaic virus (BMV)

Iron oxide nanoparticles (NP-P3) encapsulated into brome mosaic virus (BMV) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Iron oxide nanoparticles (NP-P3) encapsulated into brome mosaic virus (BMV) 0, 5000 kDa
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 10 mM KCl, 5 mM MgCl2, pH: 4.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 23
Coat Protein-Dependent Behavior of Poly(ethylene glycol) Tails in Iron Oxide Core Virus-like Nanoparticles. ACS Appl Mater Interfaces 7(22):12089-98 (2015)
Malyutin AG, Cheng H, Sanchez-Felix OR, Carlson K, Stein BD, Konarev PV, Svergun DI, Dragnea B, Bronstein LM
Dmax 25.0 nm

SASDM49 – Iron oxide nanoparticles (NP-N3) encapsulated into hepatitis B virus (HBV)

Iron oxide nanoparticles (NP-N3) encapsulated into hepatitis B virus (HBV) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Iron oxide nanoparticles (NP-N3) encapsulated into hepatitis B virus (HBV) 0, 5000 kDa
Buffer: 0.5 M LiCl, 50 mM HEPES, 2 mM DTT, pH 7.5, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 23
Coat Protein-Dependent Behavior of Poly(ethylene glycol) Tails in Iron Oxide Core Virus-like Nanoparticles. ACS Appl Mater Interfaces 7(22):12089-98 (2015)
Malyutin AG, Cheng H, Sanchez-Felix OR, Carlson K, Stein BD, Konarev PV, Svergun DI, Dragnea B, Bronstein LM
Dmax 25.5 nm

SASDA97 – PlaB

PlaB experimental SAS data
DAMMIN model
Sample: PlaB tetramer, 220 kDa Legionella pneumophila protein
Buffer: 100 mM Tris 100 mM Nacl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 15
Automated pipeline for purification, biophysical and x-ray analysis of biomacromolecular solutions. Sci Rep 5:10734 (2015)
Graewert MA, Franke D, Jeffries CM, Blanchet CE, Ruskule D, Kuhle K, Flieger A, Schäfer B, Tartsch B, Meijers R, Svergun DI
RgGuinier 4.0 nm
Dmax 10.5 nm
VolumePorod 270 nm3

SASDBL2 – MBP-PICK1 fusion

Maltose Binding Protein fused to Protein Interacting with C kinase 1 experimental SAS data
CRYSOL model
Sample: Maltose Binding Protein fused to Protein Interacting with C kinase 1 dimer, 174 kDa Homo sapiens protein
Buffer: 50 mM Tris 300 mM NaCl 1 mM maltose 1 mM EGTA 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 13
PICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner. Mol Biol Cell 26(7):1308-22 (2015)
Madasu Y, Yang C, Boczkowska M, Bethoney KA, Zwolak A, Rebowski G, Svitkina T, Dominguez R
RgGuinier 8.4 nm
Dmax 27.6 nm
VolumePorod 483 nm3

SASDAH8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

Human Filamin A Ig-like domains 20-21* experimental SAS data
DAMMIF model
Sample: Human Filamin A Ig-like domains 20-21* monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 1.9 nm
Dmax 6.8 nm
VolumePorod 32 nm3

SASDC85 – Leishmania braziliensis p23B

Leishmania braziliensis p23 isoform B experimental SAS data
DAMFILT model
Sample: Leishmania braziliensis p23 isoform B monomer, 23 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC
RgGuinier 3.0 nm
Dmax 13.0 nm

SASDCV5 – Leishmania braziliensis p23A

Uncharacterized protein experimental SAS data
DAMFILT model
Sample: Uncharacterized protein monomer, 22 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC
RgGuinier 3.3 nm
Dmax 13.0 nm