Browse by ORGANISM: other species

SASDAF4 – DmMfe2

Peroxisomal multifunctional enzyme type 2 experimental SAS data
Peroxisomal multifunctional enzyme type 2 Kratky plot
Sample: Peroxisomal multifunctional enzyme type 2 dimer, 128 kDa Drosophila melanogaster protein
Buffer: 20 mM Sodium Phosphate 200 mM NaCl 5% (v/v) Glycerol 1mM Na2EDTA 1 mM NaN3, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Jun 12
Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering. FEBS Lett 587(4):305-10 (2013)
Mehtälä ML, Haataja TJ, Blanchet CE, Hiltunen JK, Svergun DI, Glumoff T
RgGuinier 3.6 nm
Dmax 12.0 nm

SASDDJ2 – Calcium-bound polcalcin Phl p 7

polcalcin Phl p 7 experimental SAS data
MES-FOXS model
Sample: Polcalcin Phl p 7 monomer, 9 kDa Phleum pratense protein
Buffer: 0.15M NaCl, 0.025M Hepes, pH 7.4, 100 uM Ca2+, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Dec 8
Solution structures of polcalcin Phl p 7 in three ligation states: Apo-, hemi-Mg2+-bound, and fully Ca2+-bound. Proteins 81(2):300-15 (2013)
Henzl MT, Sirianni AG, Wycoff WG, Tan A, Tanner JJ
RgGuinier 1.3 nm
Dmax 3.6 nm
VolumePorod 14 nm3

SASDBR4 – Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1)

Activator of Hsp90 ATPase-1 experimental SAS data
Leishmania braziliensis Activator of Hsp90 ATPase-1 (LbAha1) Rg histogram
Sample: Activator of Hsp90 ATPase-1 monomer, 38 kDa Leishmania braziliensis protein
Buffer: 25 mM Sodium phosphate, 50 mM NaCl, 2 mM EDTA, 1 mM β-mercaptoethanol, pH: 7
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 1
Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis has an elongated shape which allows its interaction with both N- and M-domains of Hsp90. PLoS One 8(6):e66822 (2013)
Seraphim TV, Alves MM, Silva IM, Gomes FE, Silva KP, Murta SM, Barbosa LR, Borges JC
RgGuinier 3.6 nm
Dmax 14.5 nm

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

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

SASDDK2 – Aspergillus fumigatus UDP galactopyranose mutase

Aspergillus fumigatus UDP galactopyranose mutase experimental SAS data
MES-FOXS model
Sample: Aspergillus fumigatus UDP galactopyranose mutase tetramer, 228 kDa protein
Buffer: 20 mM HEPES, 45 mM NaCl, 0.5 mM Tris(hydroxypropyl)phosphine, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2010 Apr 19
Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus. J Biol Chem 287(12):9041-51 (2012)
Dhatwalia R, Singh H, Oppenheimer M, Karr DB, Nix JC, Sobrado P, Tanner JJ
RgGuinier 4.7 nm
Dmax 14.7 nm
VolumePorod 308 nm3