SASDA95 – CHD4 (CC-AH-D)

Human Chromatin Remodeler CHD4 (494-1353) experimental SAS data
DAMMIF model
Sample: Human Chromatin Remodeler CHD4 (494-1353) monomer, 101 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 Nov 13
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
Watson AA, Mahajan P, Mertens HD, Deery MJ, Zhang W, Pham P, Du X, Bartke T, Zhang W, Edlich C, Berridge G, Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, La...
RgGuinier 4.0 nm
Dmax 14.5 nm

SASDAA5 – CHD4 (AH)

Human Chromatin Remodeler CHD4 (685-1233) experimental SAS data
DAMMIF model
Sample: Human Chromatin Remodeler CHD4 (685-1233) monomer, 63 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 Nov 13
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
Watson AA, Mahajan P, Mertens HD, Deery MJ, Zhang W, Pham P, Du X, Bartke T, Zhang W, Edlich C, Berridge G, Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, La...
RgGuinier 4.0 nm
Dmax 14.5 nm

SASDAH5 – Complex of Hfq with DsrA

RNA chaperone HfqRNA DsrA experimental SAS data
SASREF model
Sample: RNA chaperone Hfq hexamer, 67 kDa Escherichia coli protein
RNA DsrA monomer, 12 kDa RNA
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 16
Structural flexibility of RNA as molecular basis for Hfq chaperone function. Nucleic Acids Res 40(16):8072-84 (2012)
Ribeiro Ede A Jr, Beich-Frandsen M, Konarev PV, Shang W, Vecerek B, Kontaxis G, Hämmerle H, Peterlik H, Svergun DI, Bläsi U, Djinović-Carugo K
RgGuinier 4.3 nm
Dmax 14.5 nm
VolumePorod 210 nm3

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

4338 hits found.