SASDLR7 – The HC Fragment of Tetanus Toxin

Hc fragment of Tetanus toxin experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Hc fragment of Tetanus toxin dimer, 103 kDa Clostridium tetani (strain … protein
Buffer: 50 mM sodium phosphate buffer, 300 mM NaCl, pH: 7.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 May 14
The HC fragment of tetanus toxin forms stable, concentration-dependent dimers via an intermolecular disulphide bond. J Mol Biol 365(1):123-34 (2007)
Qazi O, Bolgiano B, Crane D, Svergun DI, Konarev PV, Yao ZP, Robinson CV, Brown KA, Fairweather N
RgGuinier 4.0 nm
Dmax 13.2 nm
VolumePorod 150 nm3

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 EMBL X33, DORIS III, DESY 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

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 EMBL X33, DORIS III, DESY 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

SASDAQ5 – Lumazine Synthase

Lumazine Synthase experimental SAS data
DAMMIN model
Sample: Lumazine Synthase , 960 kDa Bacillus subtilis protein
Buffer: Borate buffer, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 25
Multiple assembly states of lumazine synthase: a model relating catalytic function and molecular assembly. J Mol Biol 362(4):753-70 (2006)
Zhang X, Konarev PV, Petoukhov MV, Svergun DI, Xing L, Cheng RH, Haase I, Fischer M, Bacher A, Ladenstein R, Meining W
RgGuinier 6.2 nm
Dmax 15.5 nm
VolumePorod 1450 nm3

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 EMBL X33, DORIS III, DESY 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

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 EMBL X33, DORIS III, DESY 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

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 EMBL X33, DORIS III, DESY 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

SASDM87 – Mouse ProNGF - pro-form of the NGF (nerve growth factor)

Mouse ProNGF - pro-form of the NGF (nerve growth factor) experimental SAS data
DAMMIN model
Sample: Mouse ProNGF - pro-form of the NGF (nerve growth factor) dimer, 100 kDa Mus musculus protein
Buffer: 50 mM Na-phosphate, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jul 18
Structural and functional properties of mouse proNGF. Biochem Soc Trans 34(Pt 4):605-6 (2006)
Paoletti F, Konarev PV, Covaceuszach S, Schwarz E, Cattaneo A, Lamba D, Svergun DI
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 97 nm3

SASDAR4 – PTB full

Polypyrimidine tract-binding protein 1 experimental SAS data
BUNCH model
Sample: Polypyrimidine tract-binding protein 1 monomer, 57 kDa Homo sapiens protein
Buffer: 25 mM Tris 100 mM NaCl 5.0 mM DTT, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Feb 11
Conformation of polypyrimidine tract binding protein in solution. Structure 14(6):1021-7 (2006)
Petoukhov MV, Monie TP, Allain FH, Matthews S, Curry S, Svergun DI
RgGuinier 4.0 nm
Dmax 16.5 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 EMBL X33, DORIS III, DESY 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

4657 hits found.