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246 hits found for X33

SASDA32 – BSA in HEPES

Human Serum Albumin experimental SAS data
DAMMIF model
Sample: Human Serum Albumin monomer, Homo sapiens lipid
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 12
Standard proteins
Darja Ruskule
RgGuinier 2.9 nm
Dmax 9.3 nm
VolumePorod 97 nm3

SASDC32 – Ethylene Receptor 1 Cytosolic Domain (in 250 mM NDSB)

Ethylene Receptor 1 experimental SAS data
Ethylene Receptor 1 Cytosolic Domain (in 250 mM NDSB) Rg histogram
Sample: Ethylene Receptor 1 dimer, 129 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris-NDSB 150 mM NaCl 1mM DTT 250 mM NDSB, pH: 8.8
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Mar 19
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 4.7 nm
Dmax 15.8 nm
VolumePorod 316 nm3

SASDA52 – Alcohol dehydrogenase in PBS

Alcohol dehydrogenase 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alcohol dehydrogenase 1 tetramer, 147 kDa Saccharomyces cerevisiae protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 20
Standard proteins
Darja Ruskule
RgGuinier 3.2 nm
Dmax 8.9 nm
VolumePorod 178 nm3

SASDC52 – Bruton tyrosine kinase

Tyrosine-protein kinase BTK (R28C mutant) experimental SAS data
GASBOR model
Sample: Tyrosine-protein kinase BTK (R28C mutant) monomer, 76 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl, 2 mM DTT and 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2002 Apr 2
Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering. EMBO J 22(18):4616-24 (2003)
Márquez JA, Smith CI, Petoukhov MV, Lo Surdo P, Mattsson PT, Knekt M, Westlund A, Scheffzek K, Saraste M, Svergun DI
RgGuinier 5.0 nm
Dmax 20.0 nm
VolumePorod 130 nm3

SASDA62 – bAmylase in PBS

Beta-amylase experimental SAS data
DAMMIF model
Sample: Beta-amylase tetramer, 224 kDa Ipomoea batatas protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 20
Standard proteins
Darja Ruskule
RgGuinier 4.2 nm
Dmax 12.7 nm
VolumePorod 214 nm3

SASDA82 – Apoferritin in PBS and glycerol

Ferritin light chain experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ferritin light chain 24-mer, 479 kDa Equus caballus protein
Buffer: PBS, 50% Glycerol, 0.076 M NaCl, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 20
Standard proteins
Darja Ruskule
RgGuinier 6.8 nm
Dmax 12.8 nm
VolumePorod 619 nm3

SASDF82 – Urokinase plasminogen activator surface receptor, uPAR H47C-N259C, complex with urokinase-type plasminogen activator (Amino Terminal Fragment, ATF).

Urokinase plasminogen activator surface receptorUrokinase-type plasminogen activator (Amino Terminal Fragment) experimental SAS data
DAMMIN model
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
Urokinase-type plasminogen activator (Amino Terminal Fragment) monomer, 16 kDa Homo sapiens protein
Buffer: 20 mM PBS, 5 %(v/v) glycerol, 50 mM NaSO4,, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Jun 18
Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond? J Biol Chem (2019)
Leth JM, Mertens HDT, Leth-Espensen KZ, Jørgensen TJD, Ploug M
RgGuinier 2.6 nm
Dmax 8.2 nm
VolumePorod 102 nm3

SASDA92 – Catalase in PBS

Catalase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Catalase tetramer, 240 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 17
Standard proteins
Darja Ruskule
RgGuinier 4.1 nm
Dmax 10.9 nm
VolumePorod 296 nm3

SASDJ92 – S. epidermidis extracellular matrix binding protein (Embp) F-repeats

Extracellular matrix binding protein F-repeats experimental SAS data
SASREF model
Sample: Extracellular matrix binding protein F-repeats , 70 kDa Staphylococcus epidermidis protein
Buffer: 50 mM MES, 150 mM NaCl, pH: 6
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Dec 15
A Giant Extracellular Matrix Binding Protein of Staphylococcus epidermidis Binds Surface-Immobilized Fibronectin via a Novel Mechanism. mBio 11(5) (2020)
Büttner H, Perbandt M, Kohler T, Kikhney A, Wolters M, Christner M, Heise M, Wilde J, Weißelberg S, Both A, Betzel C, Hammerschmidt S, Svergun D, Aepfelbacher M, Rohde H
RgGuinier 7.0 nm
Dmax 28.0 nm

SASDN92 – Apoform of glyceraldehyde-3-phosphate dehydrogenase (apo-kmGAPDH1p)

Glyceraldehyde-3-phosphate dehydrogenase 1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Glyceraldehyde-3-phosphate dehydrogenase 1 tetramer, 142 kDa Kluyveromyces marxianus protein
Buffer: 150 mM NaCl, 1 mM beta-mercaptoethanol, 1 mM EDTA, 10 mM TrisHCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Mar 27
The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures Journal of Biological Chemistry 281(44):33433-33440 (2006)
Ferreira-da-Silva F, Pereira P, Gales L, Roessle M, Svergun D, Moradas-Ferreira P, Damas A
RgGuinier 4.2 nm
Dmax 12.0 nm
VolumePorod 234 nm3

SASDAA2 – Conalbumin in PBS

Ovotransferrin experimental SAS data
DAMMIF model
Sample: Ovotransferrin monomer, 78 kDa Gallus gallus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 21
Standard proteins
Darja Ruskule
RgGuinier 3.8 nm
Dmax 11.0 nm
VolumePorod 117 nm3

SASDNA2 – Glyceraldehyde-3-phosphate dehydrogenase (apo-kmGAPDH1p) upon NAD+ binding

Glyceraldehyde-3-phosphate dehydrogenase 1 bound to NAD+ experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Glyceraldehyde-3-phosphate dehydrogenase 1 bound to NAD+ tetramer, 142 kDa Kluyveromyces marxianus protein
Buffer: 150 mM NaCl, 1 mM beta-mercaptoethanol, 1 mM EDTA, 10 mM TrisHCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Mar 27
The Crystal and Solution Structures of Glyceraldehyde-3-phosphate Dehydrogenase Reveal Different Quaternary Structures Journal of Biological Chemistry 281(44):33433-33440 (2006)
Ferreira-da-Silva F, Pereira P, Gales L, Roessle M, Svergun D, Moradas-Ferreira P, Damas A
RgGuinier 3.7 nm
Dmax 9.9 nm
VolumePorod 202 nm3

SASDNB2 – Human NK inhibitory receptor IRp60 with an immunoglobulin-like fold

CMRF35-like molecule 8 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: CMRF35-like molecule 8 monomer, 12 kDa Homo sapiens protein
Buffer: MES buffer with 3mM DTT, pH: 5.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Apr 6
Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a) International Journal of Biological Macromolecules 40(3):193-200 (2007)
Dimasi N, Roessle M, Moran O, Candiano G, Svergun D, Biassoni R
RgGuinier 2.0 nm
Dmax 7.0 nm
VolumePorod 22 nm3

SASDAC2 – Lyz in Sodium Acetate

Lysozyme C experimental SAS data
CRYSOL model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM Sodium Acetate, pH: 3.8
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 21
Standard proteins
Darja Ruskule
RgGuinier 1.5 nm
Dmax 4.0 nm
VolumePorod 17 nm3

SASDNC2 – NNGH-inhibited, cadmium(II)-substituted Phe171Asp/Glu219Ala double mutant of FL-MMP- 12

Macrophage metalloelastase experimental SAS data
NNGH-inhibited, cadmium(II)-substituted Phe171Asp/Glu219Ala double mutant of FL-MMP- 12 Rg histogram
Sample: Macrophage metalloelastase monomer, 54 kDa Homo sapiens protein
Buffer: 20 mM Tris10 mM CaCl2, 0.3 M NaCl, 0.2 M AHA, pH: 7.2
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 2
Evidence of Reciprocal Reorientation of the Catalytic and Hemopexin-Like Domains of Full-Length MMP-12 Journal of the American Chemical Society 130(22):7011-7021 (2008)
Bertini I, Calderone V, Fragai M, Jaiswal R, Luchinat C, Melikian M, Mylonas E, Svergun D
RgGuinier 3.2 nm
Dmax 11.0 nm
VolumePorod 58 nm3

SASDED2 – Polyglutamine tract-binding protein 1 (PQBP-1)

Polyglutamine-binding protein 1 experimental SAS data
Polyglutamine tract-binding protein 1 (PQBP-1) Rg histogram
Sample: Polyglutamine-binding protein 1 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1mM DTT,, pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Nov 18
Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. Biophys J 102(7):1608-16 (2012)
Rees M, Gorba C, de Chiara C, Bui TT, Garcia-Maya M, Drake AF, Okazawa H, Pastore A, Svergun D, Chen YW
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 51 nm3

SASDND2 – The monomeric state of b-sandwich cupredoxin Plastocyanin (Pc)

Plastocyanin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Plastocyanin monomer, 11 kDa Phormidium laminosum protein
Buffer: pure water, pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2009 May 7
Metal-Mediated Self-Assembly of a β-Sandwich Protein Chemistry - A European Journal 15(46):12672-12680 (2009)
Crowley P, Matias P, Khan A, Roessle M, Svergun D
RgGuinier 1.4 nm
Dmax 4.5 nm
VolumePorod 15 nm3

SASDNE2 – The dimeric state of b-sandwich cupredoxin Plastocyanin (Pc)

Plastocyanin experimental SAS data
REFMAC model
Sample: Plastocyanin dimer, 23 kDa Phormidium laminosum protein
Buffer: pure water, pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2009 May 7
Metal-Mediated Self-Assembly of a β-Sandwich Protein Chemistry - A European Journal 15(46):12672-12680 (2009)
Crowley P, Matias P, Khan A, Roessle M, Svergun D
RgGuinier 2.3 nm
Dmax 8.5 nm
VolumePorod 28 nm3

SASDAG2 – Lyz in Sodium Acetate

Lysozyme C experimental SAS data
GASBOR model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM Sodium Acetate, pH: 3.8
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 21
Standard proteins
Darja Ruskule
RgGuinier 1.5 nm
Dmax 4.0 nm
VolumePorod 21 nm3

SASDPG2 – Spiegelmer NOX-E36, 1.15 mg/ml

Spiegelmer NOX-E36 experimental SAS data
MC-FOLD | MC-SYM model
Sample: Spiegelmer NOX-E36 monomer, 13 kDa synthetic construct RNA
Buffer: 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Feb 20
Spiegelmers® NOX-E36 and NOX-A12
Al Kikhney, Bara Schmidt
RgGuinier 2.1 nm
Dmax 8.0 nm
VolumePorod 18 nm3

SASDAH2 – Myo in PBS

Myoglobin experimental SAS data
CRYSOL model
Sample: Myoglobin monomer, 17 kDa Equus caballus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 20
Standard proteins
Darja Ruskule
RgGuinier 1.7 nm
Dmax 5.0 nm
VolumePorod 32 nm3

SASDPH2 – Spiegelmer NOX-E36, 4.46 mg/ml

Spiegelmer NOX-E36 experimental SAS data
MC-FOLD | MC-SYM model
Sample: Spiegelmer NOX-E36 monomer, 13 kDa synthetic construct RNA
Buffer: 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Feb 20
Spiegelmers® NOX-E36 and NOX-A12
Al Kikhney, Bara Schmidt
RgGuinier 2.1 nm

SASDPJ2 – Spiegelmer NOX-A12, 1.0 mg/ml

Spiegelmer NOX-A12 experimental SAS data
MC-FOLD | MC-SYM model
Sample: Spiegelmer NOX-A12 monomer, 15 kDa synthetic construct RNA
Buffer: 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Feb 20
Spiegelmers® NOX-E36 and NOX-A12
Al Kikhney, Bara Schmidt
RgGuinier 2.1 nm
Dmax 7.8 nm
VolumePorod 21 nm3

SASDAK2 – Myo in PBS

Myoglobin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myoglobin monomer, 17 kDa Equus caballus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 20
Standard proteins
Darja Ruskule
RgGuinier 1.6 nm
Dmax 5.0 nm
VolumePorod 32 nm3

SASDPK2 – Spiegelmer NOX-A12, 3.5 mg/ml

Spiegelmer NOX-A12 experimental SAS data
MC-FOLD | MC-SYM model
Sample: Spiegelmer NOX-A12 monomer, 15 kDa synthetic construct RNA
Buffer: 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Feb 20
Spiegelmers® NOX-E36 and NOX-A12
Al Kikhney, Bara Schmidt
RgGuinier 2.0 nm
Dmax 7.6 nm
VolumePorod 18 nm3

SASDAL2 – Ovalbumin in PBS

Ovalbumin experimental SAS data
DAMMIN model
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 2.5 nm
Dmax 7.8 nm
VolumePorod 74 nm3

SASDAN2 – RNase in PBS

Ribonuclease pancreatic experimental SAS data
GASBOR model
Sample: Ribonuclease pancreatic monomer, 16 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 1.6 nm
Dmax 5.0 nm
VolumePorod 15 nm3

SASDNN2 – Experimental SAXS data for hemoglobin conjucted with six-seven copies of PEG dimer (Hb2) at concentration c = 21 mg/ml

Human hemoglobin conjugated with six-seven copies of 5-kDa PEG experimental SAS data
Human hemoglobin conjugated with six-seven copies of 5-kDa PEG Kratky plot
Sample: Human hemoglobin conjugated with six-seven copies of 5-kDa PEG dimer, 62 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 3.0 nm

SASDNP2 – Experimental SAXS data for hemoglobin conjucted with six-seven copies of PEG dimer (Hb5)

Human hemoglobin conjugated with six-seven copies of 5-kDa PEG experimental SAS data
GASBOR model
Sample: Human hemoglobin conjugated with six-seven copies of 5-kDa PEG dimer, 62 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 3.3 nm
Dmax 13.0 nm

SASDAQ2 – Ubiquitin in sodium acetate

Ubiquitin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ubiquitin monomer, 9 kDa Bos taurus protein
Buffer: 40 mM Sodium acetate 150 mM NaCl, pH: 5.5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 1.3 nm
Dmax 4.9 nm
VolumePorod 12 nm3

SASDNQ2 – Experimental SAXS data for hemoglobin conjucted with two copies of PEG dimer (Hb2) at concentration c = 25 mg/ml

Human hemoglobin conjugated with two copies of 5-kDa PEG experimental SAS data
Human hemoglobin conjugated with two copies of 5-kDa PEG Kratky plot
Sample: Human hemoglobin conjugated with two copies of 5-kDa PEG dimer, 62 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 2.4 nm

SASDAR2 – RNase in PBS

Ribonuclease pancreatic experimental SAS data
DAMMIF model
Sample: Ribonuclease pancreatic monomer, 16 kDa Bos taurus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Sep 18
Standard proteins
Darja Ruskule
RgGuinier 1.6 nm
Dmax 5.0 nm
VolumePorod 17 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 ...X33, DORIS III 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

SASDNR2 – Experimental SAXS data for hemoglobin conjucted with two copies of PEG dimer (Hb2)

Human hemoglobin conjugated with two copies of 5-kDa PEG experimental SAS data
GASBOR model
Sample: Human hemoglobin conjugated with two copies of 5-kDa PEG dimer, 62 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 2.8 nm
Dmax 13.0 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 ...X33, DORIS III 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

SASDNS2 – Experimental SAXS data for native hemoglobin (Hb) at concentration c = 5 mg/ml

Hemoglobin subunit gamma-2 experimental SAS data
GASBOR model
Sample: Hemoglobin subunit gamma-2 monomer, 31 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 2.4 nm
Dmax 13.0 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 ...X33, DORIS III 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

SASDNT2 – Experimental SAXS data for native hemoglobin (Hb) at concentration c = 31.25 mg/ml

Hemoglobin subunit gamma-2 experimental SAS data
Hemoglobin subunit gamma-2 Kratky plot
Sample: Hemoglobin subunit gamma-2 monomer, 31 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 2.2 nm

SASDMU2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.1 nm
Dmax 20.5 nm

SASDNU2 – Homodimerization of a membrane type 1 matrix metalloproteinase (MT1-MMP)

HemopexinHemopexin experimental SAS data
CUSTOM IN-HOUSE model
Sample: Hemopexin monomer, 23 kDa Homo sapiens protein
Hemopexin dimer, 46 kDa Homo sapiens protein
Buffer: 50 mM HEPES, 150 mM NaCl, 10 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Nov 25
The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain Journal of Biological Chemistry 286(9):7587-7600 (2011)
Tochowicz A, Goettig P, Evans R, Visse R, Shitomi Y, Palmisano R, Ito N, Richter K, Maskos K, Franke D, Svergun D, Nagase H, Bode W, Itoh Y
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 48 nm3

SASDMV2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) monomer, 220 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 7.5 nm
Dmax 25.5 nm

SASDNV2 – The pro-convertase formed by human FB and cobra venom factor (CVF)

Cobra venom factor experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cobra venom factor monomer, 185 kDa Naja kaouthia protein
Buffer: 10 mM Tris 5 mM MgCl2 10 mM NaCl, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Dec 19
Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex The EMBO Journal 28(16):2469-2478 (2009)
Janssen B, Gomes L, Koning R, Svergun D, Koster A, Fritzinger D, Vogel C, Gros P
RgGuinier 4.6 nm
Dmax 15.0 nm
VolumePorod 384 nm3

SASDMW2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.4 nm
Dmax 22.5 nm

SASDNW2 – Human Anti-TSC Recombinant Antibody (Fab MOR03268)

Fab fragment in complex with small molecule hapten, crystal form-1 experimental SAS data
DAMMIN model
Sample: Fab fragment in complex with small molecule hapten, crystal form-1 monomer, 45 kDa Homo sapiens protein
Buffer: 20 mM Tris–HCl, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2005 Jul 25
Fab MOR03268 Triggers Absorption Shift of a Diagnostic Dye via Packaging in a Solvent-shielded Fab Dimer Interface Journal of Molecular Biology 377(1):206-219 (2008)
Hillig R, Urlinger S, Fanghänel J, Brocks B, Haenel C, Stark Y, Sülzle D, Svergun D, Baesler S, Malawski G, Moosmayer D, Menrad A, Schirner M, Licha K
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 71 nm3

SASDAX2 – Pyruvate decarboxylase (PDC) from Z. mobilis

Pyruvate decarboxylase experimental SAS data
CRYSOL model
Sample: Pyruvate decarboxylase tetramer, 244 kDa Zymomonas mobilis protein
Buffer: 100 mM Sodium Citrate, 17% Glycerol, 22.5% PEG 1500, pH: 6
Experiment: SAXS data collected at ...X33, DORIS III on 1998 Nov 3
Crystal versus solution structures of thiamine diphosphate-dependent enzymes. J Biol Chem 275(1):297-302 (2000)
Svergun DI, Petoukhov MV, Koch MH, König S
RgGuinier 3.9 nm
Dmax 11.0 nm

SASDMX2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) monomer, 225 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 10.0 nm
Dmax 21.9 nm

SASDNX2 – Human Anti-TSC Recombinant Antibody (Fab MOR03268) bound to TSC ligand

Fab fragment in complex with small molecule hapten, crystal form-1(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL experimental SAS data
DAMMIN model
Sample: Fab fragment in complex with small molecule hapten, crystal form-1 monomer, 45 kDa Homo sapiens protein
(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL monomer, 0 kDa
Buffer: 20 mM Tris–HCl, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2005 Jul 27
Fab MOR03268 Triggers Absorption Shift of a Diagnostic Dye via Packaging in a Solvent-shielded Fab Dimer Interface Journal of Molecular Biology 377(1):206-219 (2008)
Hillig R, Urlinger S, Fanghänel J, Brocks B, Haenel C, Stark Y, Sülzle D, Svergun D, Baesler S, Malawski G, Moosmayer D, Menrad A, Schirner M, Licha K
RgGuinier 4.1 nm
Dmax 16.0 nm
VolumePorod 139 nm3

SASDMY2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.5 nm
Dmax 22.9 nm

SASDNY2 – Human Anti-TSC Recombinant Antibody (Fab MOR03268) with TSC ligand excess

Fab fragment in complex with small molecule hapten, crystal form-1(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Fab fragment in complex with small molecule hapten, crystal form-1 monomer, 45 kDa Homo sapiens protein
(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL monomer, 0 kDa
Buffer: 20 mM Tris–HCl, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2005 Jul 25
Fab MOR03268 Triggers Absorption Shift of a Diagnostic Dye via Packaging in a Solvent-shielded Fab Dimer Interface Journal of Molecular Biology 377(1):206-219 (2008)
Hillig R, Urlinger S, Fanghänel J, Brocks B, Haenel C, Stark Y, Sülzle D, Svergun D, Baesler S, Malawski G, Moosmayer D, Menrad A, Schirner M, Licha K
RgGuinier 3.6 nm
Dmax 15.0 nm
VolumePorod 107 nm3

SASDMZ2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 6.9 nm
Dmax 23.8 nm

SASDNZ2 – Tetrameric state of soluble endoglin receptor

Endoglin experimental SAS data
DAMMIF model
Sample: Endoglin tetramer, 243 kDa Homo sapiens protein
Buffer: 10 mM Tris–HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2008 Oct 17
Structural and functional characterization of soluble endoglin receptor Biochemical and Biophysical Research Communications 383(4):386-391 (2009)
Le B, Franke D, Svergun D, Han T, Hwang H, Kim K
RgGuinier 7.6 nm
Dmax 26.0 nm
VolumePorod 434 nm3

SASDM23 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 16
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 5.9 nm
Dmax 19.7 nm

SASDN23 – Homodimeric state of soluble endoglin receptor

Endoglin experimental SAS data
DAMMIF model
Sample: Endoglin dimer, 121 kDa Homo sapiens protein
Buffer: 10 mM Tris–HCl, 50 mM NaCl, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2008 Oct 17
Structural and functional characterization of soluble endoglin receptor Biochemical and Biophysical Research Communications 383(4):386-391 (2009)
Le B, Franke D, Svergun D, Han T, Hwang H, Kim K
RgGuinier 4.7 nm
Dmax 17.0 nm
VolumePorod 173 nm3

SASDM33 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) experimental SAS data
DAMMIF model
Sample: Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) monomer, 125 kDa
Buffer: phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment: SAXS data collected at ...X33, DORIS III on 2012 Aug 19
Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI
RgGuinier 5.5 nm
Dmax 18.3 nm

SASDN63 – Microtubule affinity regulating kinase (isoform MARK2, T208E point mutant)

Serine/threonine-protein kinase MARK2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Serine/threonine-protein kinase MARK2 monomer, 36 kDa Homo sapiens protein
Buffer: 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 May 16
Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E
RgGuinier 2.4 nm
Dmax 8.0 nm
VolumePorod 61 nm3

SASDM73 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 0%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.5 nm

SASDN73 – Microtubule affinity regulating kinase (isoform MARK2, wild type)

Serine/threonine-protein kinase MARK2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Serine/threonine-protein kinase MARK2 monomer, 36 kDa Homo sapiens protein
Buffer: 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 May 16
Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 62 nm3

SASDM83 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 60%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.2 nm

SASDN83 – Microtubule affinity regulating kinase (isoform MARK1)

Serine/threonine-protein kinase MARK1 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Serine/threonine-protein kinase MARK1 monomer, 37 kDa Homo sapiens protein
Buffer: 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH: 6.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 May 16
Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2 Journal of Biological Chemistry 281(37):27586-27599 (2006)
Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 64 nm3

SASDM93 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 100%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.1 nm

SASDN93 – Dystrophiamyotonica kinase (DMPK)

Myotonin-protein kinase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myotonin-protein kinase monomer, 92 kDa Homo sapiens protein
Buffer: 50 mM TrisHCl 50mM NaCl, 2.5 mM-mercaptoethanol, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2005 Mar 18
Molecular insights into the self‐assembly mechanism of dystrophia myotonica kinase The FASEB Journal 20(8):1142-1151 (2006)
Garcia P, Ucurum Z, Bucher R, Svergun D, Huber T, Lustig A, Konarev P, Marino M, Mayans O
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 173 nm3

SASDMA3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 100%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 100%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 12
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 3.3 nm

SASDMB3 – Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%)

Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) experimental SAS data
DAMMIN model
Sample: Native tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 80%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 0.9 nm
Dmax 3.3 nm

SASDBC3 – RepB, the replication initiator protein of a promiscuous Streptococcal plasmid pMV158

Replication initiator protein of a promiscuous streptococcal plasmid pMV158. experimental SAS data
NONE model
Sample: Replication initiator protein of a promiscuous streptococcal plasmid pMV158. hexamer, Streptococcus sp. protein
Buffer: 10 mM TRIS 5 mM EDTA 1.0 M KCl, pH: 8.5
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Jun 16
Conformational plasticity of RepB, the replication initiator protein of promiscuous streptococcal plasmid pMV158. Sci Rep 6:20915 (2016)
Boer DR, Ruiz-Masó JA, Rueda M, Petoukhov MV, Machón C, Svergun DI, Orozco M, del Solar G, Coll M
RgGuinier 3.8 nm
Dmax 10.6 nm
VolumePorod 282 nm3

SASDMC3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 0%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 0%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.3 nm
Dmax 4.5 nm

SASDMD3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 20%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 20%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 20%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 20%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.1 nm
Dmax 3.5 nm

SASDME3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 60%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 60%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Nov 24
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.0 nm
Dmax 2.9 nm

SASDLF3 – Staphylococcal immunoglobulin-binding protein bound to complement component C3

Protein A experimental SAS data
DAMMIN model
Sample: Protein A monomer, 28 kDa Staphylococcus aureus protein
Buffer: 10 mM HEPES, pH 7.2, 3 mM EDTA, pH: 7.2
Experiment: SAXS data collected at ...X33, DORIS III on 2005 May 12
A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d Molecular Immunology 48(4):452-462 (2011)
Clark E, Crennell S, Upadhyay A, Zozulya A, Mackay J, Svergun D, Bagby S, van den Elsen J
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 81 nm3

SASDMF3 – Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%)

Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) experimental SAS data
DAMMIN model
Sample: Oxidized tannin macromolecules (DP7, average polymerization 6.3) in water-ethanol solution (water fraction 80%) heptamer, 2 kDa
Buffer: water-ethanol solution (water fraction 80%), pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 12
Rigidity, conformation, and solvation of native and oxidized tannin macromolecules in water-ethanol solution. J Chem Phys 130(24):245103 (2009)
Zanchi D, Konarev PV, Tribet C, Baron A, Svergun DI, Guyot S
RgGuinier 1.2 nm
Dmax 3.6 nm

SASDLG3 – Thermoplasma E2 catalytic core

Regulatory protein E2 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Regulatory protein E2 , 1037 kDa Human papillomavirus type … protein
Buffer: 50 mM Tris ⁄ HCl, pH 8.8, 100 mM NaCl, pH: 8.8
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Jul 13
The catalytic core of an archaeal 2-oxoacid dehydrogenase multienzyme complex is a 42-mer protein assembly FEBS Journal 279(5):713-723 (2012)
Marrott N, Marshall J, Svergun D, Crennell S, Hough D, Danson M, van den Elsen J
RgGuinier 8.8 nm
Dmax 22.0 nm
VolumePorod 2473 nm3

SASDLH3 – Truncated Thermoplasma E2 catalytic core

Regulatory protein E2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Regulatory protein E2 trimer, 73 kDa Human papillomavirus type … protein
Buffer: 50 mM Tris ⁄ HCl, pH 8.8, 100 mM NaCl, pH: 8.8
Experiment: SAXS data collected at ...X33, DORIS III on 2011 May 27
Why are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complex Biochemical Journal 463(3):405-412 (2014)
Marrott N, Marshall J, Svergun D, Crennell S, Hough D, van den Elsen J, Danson M
RgGuinier 3.1 nm
Dmax 11.0 nm
VolumePorod 149 nm3

SASDAQ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 28.0 nm
VolumePorod 700 nm3

SASDAR3 – PsrP functional binding region

Functional binding region (187-385) of the pneumococcal serine-rich repeat protein experimental SAS data
PsrP functional binding region Rg histogram
Sample: Functional binding region (187-385) of the pneumococcal serine-rich repeat protein monomer, 22 kDa Streptococcus pneumoniae protein
Buffer: 20 mM sodium citrate 250 mM NaCl 2.5 % Glycerol, pH: 5.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Jul 2
The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold. Open Biol 4:130090 (2014)
Schulte T, Löfling J, Mikaelsson C, Kikhney A, Hentrich K, Diamante A, Ebel C, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 2.3 nm
Dmax 7.7 nm
VolumePorod 37 nm3

SASDAS3 – Fila16-17

immunoglobulin- like filamin two-domain fragment 16-17 experimental SAS data
GASBOR model
Sample: immunoglobulin- like filamin two-domain fragment 16-17 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 33 nm3

SASDAT3 – Fila18-19

immunoglobulin- like filamin two-domain fragment 18-19 experimental SAS data
GASBOR model
Sample: immunoglobulin- like filamin two-domain fragment 18-19 monomer, 20 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 34 nm3

SASDAU3 – Fila22-23

immunoglobulin- like filamin two-domain fragment 22-23 experimental SAS data
GASBOR model
Sample: immunoglobulin- like filamin two-domain fragment 22-23 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 32 nm3

SASDAV3 – Geminin:Cdt1 2:1 heterotrimer

GemininDNA replication factor Cdt1 experimental SAS data
CRYSOL model
Sample: Geminin dimer, 47 kDa Homo sapiens protein
DNA replication factor Cdt1 monomer, 60 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Aug 13
Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proc Natl Acad Sci U S A 106(47):19807-12 (2009)
De Marco V, Gillespie PJ, Li A, Karantzelis N, Christodoulou E, Klompmaker R, van Gerwen S, Fish A, Petoukhov MV, Iliou MS, Lygerou Z, Medema RH, Blow JJ, Svergun DI, Taraviras S, Perrakis A
RgGuinier 2.9 nm
Dmax 10.0 nm
VolumePorod 70 nm3

SASDAW3 – Geminin:Cdt1 4:2 heterohexamer

GemininDNA replication factor Cdt1 experimental SAS data
CRYSOL model
Sample: Geminin dimer, 47 kDa Homo sapiens protein
DNA replication factor Cdt1 monomer, 60 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Oct 5
Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing. Proc Natl Acad Sci U S A 106(47):19807-12 (2009)
De Marco V, Gillespie PJ, Li A, Karantzelis N, Christodoulou E, Klompmaker R, van Gerwen S, Fish A, Petoukhov MV, Iliou MS, Lygerou Z, Medema RH, Blow JJ, Svergun DI, Taraviras S, Perrakis A
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 120 nm3

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.5 nm
Dmax 29.0 nm
VolumePorod 750 nm3

SASDAY3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.3 nm
Dmax 29.0 nm
VolumePorod 720 nm3

SASDAZ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.0 nm

SASDA24 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 27.0 nm

SASDA54 – RNA Aptamer

SRB2m experimental SAS data
DAMMIN model
Sample: SRB2m dimer, 33 kDa RNA
Buffer: Hepes, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 24
Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
Werner A, Konarev PV, Svergun DI, Hahn U
RgGuinier 2.8 nm
Dmax 10.0 nm
VolumePorod 38 nm3

SASDA74 – RNA Aptamer

SRB2m experimental SAS data
DAMMIN model
Sample: SRB2m dimer, 33 kDa RNA
Buffer: Hepes, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 24
Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
Werner A, Konarev PV, Svergun DI, Hahn U
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 31 nm3

SASDA84 – RNA Aptamer

SRB2m experimental SAS data
DAMMIN model
Sample: SRB2m dimer, 33 kDa RNA
Buffer: Hepes, pH: 7.4
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 24
Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
Werner A, Konarev PV, Svergun DI, Hahn U
RgGuinier 2.3 nm
Dmax 8.0 nm
VolumePorod 24 nm3

SASDA94 – Der p21

Der p21, allegren experimental SAS data
DAMMIN model
Sample: Der p21, allegren dimer, 26 kDa Escherichia coli protein
Buffer: 10 mM Hepes , pH: 7
Experiment: SAXS data collected at ...X33, DORIS III on 2006 Jul 24
Characterization of Der p 21, a new important allergen derived from the gut of house dust mites. Allergy 63(6):758-67 (2008)
Weghofer M, Dall'Antonia Y, Grote M, Stöcklinger A, Kneidinger M, Balic N, Krauth MT, Fernández-Caldas E, Thomas WR, van Hage M, Vieths S, Spitzauer S, Horak F, Svergun DI, Konarev PV, Valent P, Thalh...
RgGuinier 2.7 nm
Dmax 8.5 nm
VolumePorod 50 nm3

SASDAA4 – Full length GbpA

Full length GbpA experimental SAS data
GASBOR model
Sample: Full length GbpA monomer, 54 kDa Vibrio cholerae protein
Buffer: 25 mM Tris/HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 16
The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces. PLoS Pathog 8(1):e1002373 (2012)
Wong E, Vaaje-Kolstad G, Ghosh A, Hurtado-Guerrero R, Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM
RgGuinier 3.9 nm
Dmax 14.5 nm
VolumePorod 100 nm3

SASDAB4 – Truncated GbpA

Truncated GbpA experimental SAS data
GASBOR model
Sample: Truncated GbpA monomer, 44 kDa Vibrio cholerae protein
Buffer: 25 mM Tris/HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2007 Oct 16
The Vibrio cholerae colonization factor GbpA possesses a modular structure that governs binding to different host surfaces. PLoS Pathog 8(1):e1002373 (2012)
Wong E, Vaaje-Kolstad G, Ghosh A, Hurtado-Guerrero R, Konarev PV, Ibrahim AF, Svergun DI, Eijsink VG, Chatterjee NS, van Aalten DM
RgGuinier 3.6 nm
Dmax 12.5 nm
VolumePorod 80 nm3

SASDAC4 – FilaminC 23-24

Filamin C 23-24 experimental SAS data
DAMMIN model
Sample: Filamin C 23-24 dimer, 40 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 50 mM NaCl, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2005 Jun 17
Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol 368(4):1011-23 (2007)
Sjekloća L, Pudas R, Sjöblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylänne J, Djinović Carugo K
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 75 nm3

SASDAD4 – Full length GtBP3

full length CtBP3 experimental SAS data
DAMMIN model
Sample: full length CtBP3 tetramer, 170 kDa protein
Buffer: 25 mM Tris/HCl 250 mM NaCl, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2004 Nov 18
The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci 15(5):1042-50 (2006)
Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M
RgGuinier 5.1 nm
Dmax 19.0 nm
VolumePorod 330 nm3

SASDAE4 – C-terminal CtBP3

C-term part CtBP3 experimental SAS data
DAMMIN model
Sample: C-term part CtBP3 dimer, 52 kDa protein
Buffer: 25 mM Tris/HCl 250 mM NaCl, pH: 8
Experiment: SAXS data collected at ...X33, DORIS III on 2004 Nov 18
The C-terminal domain of the transcriptional corepressor CtBP is intrinsically unstructured. Protein Sci 15(5):1042-50 (2006)
Nardini M, Svergun D, Konarev PV, Spanò S, Fasano M, Bracco C, Pesce A, Donadini A, Cericola C, Secundo F, Luini A, Corda D, Bolognesi M
RgGuinier 5.5 nm
Dmax 20.0 nm
VolumePorod 126 nm3

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 ...X33, DORIS III 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

SASDBF4 – Wild-type LytA (N-His6) with choline

Lytic Amidase with choline experimental SAS data
SASREF model
Sample: Lytic Amidase with choline dimer, 75 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 150 mM NaCl 5 mM choline chloride 1 µM ZnCl2, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Jul 2
Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae. MBio 5(1):e01120-13 (2014)
Mellroth P, Sandalova T, Kikhney A, Vilaplana F, Hesek D, Lee M, Mobashery S, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 4.9 nm
Dmax 15.0 nm
VolumePorod 115 nm3

SASDAG4 – HsMfe2

Peroxisomal multifunctional enzyme type 2 experimental SAS data
Peroxisomal multifunctional enzyme type 2 Kratky plot
Sample: Peroxisomal multifunctional enzyme type 2 dimer, 159 kDa Homo sapiens 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 ...X33, DORIS III on 2011 Mar 22
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 4.6 nm
Dmax 15.0 nm

SASDBG4 – Prophage LytA with choline

Prophage Lytic Amidase with choline experimental SAS data
SASREF model
Sample: Prophage Lytic Amidase with choline dimer, 73 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 150 mM NaCl 5 mM choline chloride 1 µM ZnCl2, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Jul 2
Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae. MBio 5(1):e01120-13 (2014)
Mellroth P, Sandalova T, Kikhney A, Vilaplana F, Hesek D, Lee M, Mobashery S, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 5.9 nm
Dmax 17.0 nm
VolumePorod 130 nm3

SASDAH4 – DH-PH

DH-PH module of PDZRhoGEF experimental SAS data
DAMMIN model
Sample: DH-PH module of PDZRhoGEF monomer, 41 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2008 Oct 30
The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA. Protein Sci 18(10):2067-79 (2009)
Cierpicki T, Bielnicki J, Zheng M, Gruszczyk J, Kasterka M, Petoukhov M, Zhang A, Fernandez EJ, Svergun DI, Derewenda U, Bushweller JH, Derewenda ZS
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 60 nm3

SASDBH4 – Wild-type LytA (N-His6) without choline

Lytic Amidase without choline experimental SAS data
SASREF model
Sample: Lytic Amidase without choline monomer, 37 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 150 mM NaCl 1 µM ZnCl2, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Jul 3
Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae. MBio 5(1):e01120-13 (2014)
Mellroth P, Sandalova T, Kikhney A, Vilaplana F, Hesek D, Lee M, Mobashery S, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 3.4 nm
Dmax 12.5 nm
VolumePorod 56 nm3

SASDAJ4 – CRM1

Exportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Feb 3
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 3.8 nm
Dmax 11.0 nm
VolumePorod 190 nm3

SASDBJ4 – Wild-type LytA choline-binding domain

Lytic Amidase choline-binding domain experimental SAS data
SASREF model
Sample: Lytic Amidase choline-binding domain dimer, 17 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 150 mM NaCl 5 mM choline chloride 1 µM ZnCl2, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2011 Dec 11
Structural and functional insights into peptidoglycan access for the lytic amidase LytA of Streptococcus pneumoniae. MBio 5(1):e01120-13 (2014)
Mellroth P, Sandalova T, Kikhney A, Vilaplana F, Hesek D, Lee M, Mobashery S, Normark S, Svergun D, Henriques-Normark B, Achour A
RgGuinier 3.3 nm
Dmax 10.0 nm
VolumePorod 49 nm3

SASDAK4 – CRM1 RanGTP

Exportin-1GTP-binding nuclear protein Ran experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at ...X33, DORIS III on 2009 Feb 3
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 3.6 nm
Dmax 10.0 nm