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

SASDM59 – brome mosaic virus (BMV)

brome mosaic virus (BMV) experimental SAS data
brome mosaic virus (BMV) Kratky plot
Sample: brome mosaic virus (BMV) monomer, 5000 kDa
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 10 mM KCl, 5 mM MgCl2, pH: 4.6
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 31.7 nm

SASDM69 – Hepatitis B virus (HBV)

Hepatitis B virus (HBV) experimental SAS data
Hepatitis B virus (HBV) Kratky plot
Sample: Hepatitis B virus (HBV) None,
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 32.0 nm

SASDA37 – Surface Protein G (SasG) EG5 repeat protein G51-G52

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 24 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 4.7 nm
Dmax 19.0 nm
VolumePorod 29 nm3

SASDA47 – Surface Protein G (SasG) EG5 repeat protein G51-G53

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 39 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 7.7 nm
Dmax 30.5 nm
VolumePorod 49 nm3

SASDA57 – Surface Protein G (SasG) EG5 repeat protein G51-G54

Surface protein G experimental SAS data
GASBOR model
Sample: Surface protein G monomer, 53 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 9.7 nm
Dmax 38.5 nm
VolumePorod 58 nm3

SASDA67 – Surface Protein G (SasG) EG5 repeat protein G51-G55

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 67 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 12.0 nm
Dmax 48.0 nm
VolumePorod 87 nm3

SASDA77 – Surface Protein G (SasG) EG5 repeat protein G51-G56

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 81 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 14.1 nm
Dmax 57.0 nm
VolumePorod 89 nm3

SASDA87 – Surface Protein G (SasG) EG5 repeat protein G51-G57

Surface protein G experimental SAS data
SASREF model
Sample: Surface protein G monomer, 95 kDa Staphylococcus aureus protein
Buffer: 20 mM Tris 200 mM NaCl 1 mM EDTA 20 mM Tris.Cl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 12
Cooperative folding of intrinsically disordered domains drives assembly of a strong elongated protein. Nat Commun 6:7271 (2015)
Gruszka DT, Whelan F, Farrance OE, Fung HK, Paci E, Jeffries CM, Svergun DI, Baldock C, Baumann CG, Brockwell DJ, Potts JR, Clarke J
RgGuinier 15.9 nm
Dmax 63.0 nm
VolumePorod 122 nm3

4692 hits found.