Browse by DISSEMINATION: Published

SASDMR2 – HPMA-Based Nanoparticles with Cholesterol (1.4%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with cholesterol 1.4% experimental SAS data
DAMFILT model
Sample: N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with cholesterol 1.4% 0, 16272 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27
Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
Filippov SK, Chytil P, Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI
RgGuinier 6.2 nm
Dmax 22.0 nm

SASDMS2 – HPMA-Based Nanoparticles with Cholesterol (2.7%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (2.7%) experimental SAS data
DAMFILT model
Sample: N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (2.7%) 0, 16740 kDa
Buffer: phosphate buffer saline (PBS) (pH 7.2), pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27
Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
Filippov SK, Chytil P, Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI
RgGuinier 5.2 nm
Dmax 28.1 nm

SASDMT2 – HPMA-Based Nanoparticles with Cholesterol (3.0%)

N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (3.0%) experimental SAS data
DAMFILT model
Sample: N-(2-hydroxypropyl)- 31 methacrylamide (HPMA) copolymers with Cholesterol (3.0%) 0, 29520 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 27
Macromolecular HPMA-based nanoparticles with cholesterol for solid-tumor targeting: detailed study of the inner structure of a highly efficient drug delivery system. Biomacromolecules 13(8):2594-604 (2012)
Filippov SK, Chytil P, Konarev PV, Dyakonova M, Papadakis C, Zhigunov A, Plestil J, Stepanek P, Etrych T, Ulbrich K, Svergun DI
RgGuinier 9.4 nm
Dmax 43.2 nm

SASDKR3 – Deuterated calmodulin bound to the HIV-1 MA protein

Calmodulin-1calcium ionsGag-Pol polyprotein experimental SAS data
MONSA model
Sample: Calmodulin-1 monomer, 17 kDa Xenopus laevis protein
Calcium ions tetramer, 0 kDa
Gag-Pol polyprotein monomer, 15 kDa Human immunodeficiency virus … protein
Buffer: 50 mM MOPS, 5 mM CaCl2, 2 mM TCEP, pH: 7.4
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2010 Jun 23
Calmodulin binds a highly extended HIV-1 MA protein that refolds upon its release. Biophys J 103(3):541-549 (2012)
Taylor JE, Chow JYH, Jeffries CM, Kwan AH, Duff AP, Hamilton WA, Trewhella J
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 55 nm3

SASDMM9 – Response Regulator RocR from Pseudomonas aeruginosa

RocR experimental SAS data
OTHER model
Sample: RocR tetramer, 171 kDa Pseudomonas aeruginosa (strain … protein
Buffer: 50 mM Tris–HCl, 250 mM NaCl, 10 mM imidazole, 5% glycerol, 0.5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 9
Structural Insights into the Regulatory Mechanism of the Response Regulator RocR from Pseudomonas aeruginosa in Cyclic Di-GMP Signaling Journal of Bacteriology 194(18):4837-4846 (2012)
Chen M, Kotaka M, Vonrhein C, Bricogne G, Rao F, Chuah M, Svergun D, Schneider G, Liang Z, Lescar J
RgGuinier 3.7 nm
Dmax 11.0 nm

SASDAE5 – CYNEX4

CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) experimental SAS data
DAMMIF model
Sample: CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) monomer, 93 kDa Homo sapiens protein
Buffer: 50 mM HEPES 150 mM NaCl 1 mM EGTA, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Sep 11
Conformational analysis of a genetically encoded FRET biosensor by SAXS. Biophys J 102(12):2866-75 (2012)
Mertens HD, Piljić A, Schultz C, Svergun DI
RgGuinier 3.7 nm
Dmax 12.8 nm
VolumePorod 135 nm3

SASDAF5 – CYNEX4-T266D

CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) T266D mutant experimental SAS data
DAMMIF model
Sample: CYNEX4 FRET probe, (eYFP-AnnexinA4-eCFP) T266D mutant monomer, 93 kDa Homo sapiens protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Sep 11
Conformational analysis of a genetically encoded FRET biosensor by SAXS. Biophys J 102(12):2866-75 (2012)
Mertens HD, Piljić A, Schultz C, Svergun DI
RgGuinier 4.1 nm
Dmax 14.4 nm
VolumePorod 146 nm3

SASDAJ5 – Annexin-A4

Annexin-A4 experimental SAS data
CRYSOL model
Sample: Annexin-A4 monomer, 36 kDa Homo sapiens protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Sep 11
Conformational analysis of a genetically encoded FRET biosensor by SAXS. Biophys J 102(12):2866-75 (2012)
Mertens HD, Piljić A, Schultz C, Svergun DI
RgGuinier 2.4 nm
Dmax 7.6 nm
VolumePorod 54 nm3

SASDM97 – Recombinant monoclonal anti-proNGF antibody in single chain Fv fragment (scFv)

Recombinant monoclonal anti-proNGF antibody in single chain Fv fragment (scFv) experimental SAS data
BUNCH model
Sample: Recombinant monoclonal anti-proNGF antibody in single chain Fv fragment (scFv) monomer, 29 kDa protein
Buffer: phosphate buffered saline, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 21
Direct intracellular selection and biochemical characterization of a recombinant anti-proNGF single chain antibody fragment. Arch Biochem Biophys 522(1):26-36 (2012)
Paoletti F, Malerba F, Konarev PV, Visintin M, Scardigli R, Fasulo L, Lamba D, Svergun DI, Cattaneo A
RgGuinier 2.7 nm
Dmax 8.0 nm
VolumePorod 39 nm3

SASDLL5 – frataxin homolog, Yfh1, at 0 °C

Frataxin homolog, mitochondrial experimental SAS data
frataxin homolog, Yfh1, at 0 °C Rg histogram
Sample: Frataxin homolog, mitochondrial monomer, 14 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM HEPES, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Nov 28
The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1. J Mol Biol 417(5):413-24 (2012)
Adrover M, Martorell G, Martin SR, Urosev D, Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A
RgGuinier 2.2 nm