Browse by ORGANISM: Mus musculus (Mouse)

SASDB36 – Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant

Myelin-associated glycoprotein (20-508; N406Q mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; N406Q mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 5
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.3 nm
Dmax 25.6 nm
VolumePorod 193 nm3

SASDB46 – Glycosylated Myelin-associated glycoprotein immunoglobulin domains 1-3

Myelin-associated glycoprotein Ig domains 1-3 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein Ig domains 1-3 monomer, 35 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 59 nm3

SASDB56 – Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) I473E mutant

Myelin-associated glycoprotein (20-508; I473E mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; I473E mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 6.0 nm
Dmax 21.2 nm
VolumePorod 100 nm3

SASDB66 – Deglycosylated myelin-associated glycoprotein full extracellular domain (Ig 1-5) N406Q mutant

Myelin-associated glycoprotein (20-508; N406Q mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; N406Q mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Jul 28
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.8 nm
Dmax 29.0 nm
VolumePorod 216 nm3

SASDB76 – Deglycosylated myelin-associated glycoprotein (immunoglobulin domains 1-3)

Myelin-associated glycoprotein Ig domains 1-3 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein Ig domains 1-3 monomer, 35 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 3.9 nm
Dmax 12.6 nm
VolumePorod 49 nm3

SASDBF6 – Deglycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

Myelin-associated glycoprotein Ig domains 1-5 experimental SAS data
NONE model
Sample: Myelin-associated glycoprotein Ig domains 1-5 dimer, 108 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 7.3 nm
Dmax 25.5 nm
VolumePorod 166 nm3

SASDBG3 – Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)

Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) experimental SAS data
DAMMIN model
Sample: Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) monomer, 40 kDa Mus musculus protein
Buffer: 20 mM Tris 150 mM NaCl 3% glycerol, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2015 Sep 27
Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding. Biochemistry 55(6):914-26 (2016)
Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T
RgGuinier 3.3 nm
Dmax 13.1 nm

SASDBH3 – Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 (fragment 30-380)

Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 experimental SAS data
DAMMIN model
Sample: Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 dimer, 80 kDa Mus musculus protein
Buffer: 20 mM Tris 150 mM NaCl 3% glycerol, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2015 Jun 28
Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding. Biochemistry 55(6):914-26 (2016)
Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T
RgGuinier 4.2 nm
Dmax 21.6 nm

SASDCJ2 – Solution structure of recombinant prion protein (89–230) in complex with Fab-P

Major prion proteinP-Clone Fab, Chimera experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Major prion protein monomer, 23 kDa Mus musculus protein
P-Clone Fab, Chimera monomer, 47 kDa Homo sapiens protein
Buffer: sodium acetate buffer (20 mM sodium acetate, pH 5.1; 150 mM NaCl), pH: 5.1
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2013 Dec 5
Prion Protein-Antibody Complexes Characterized by Chromatography-Coupled Small-Angle X-Ray Scattering. Biophys J 109(4):793-805 (2015)
Carter L, Kim SJ, Schneidman-Duhovny D, Stöhr J, Poncet-Montange G, Weiss TM, Tsuruta H, Prusiner SB, Sali A
RgGuinier 3.9 nm
Dmax 14.5 nm
VolumePorod 106 nm3

SASDAG7 – CD44 HABD scFv MEM-85 complex

Hyaluronate binding domain of CD44 antigenSingle-chain Variable Fragment of Antibody MEM-85 experimental SAS data
DAMMIN model
Sample: Hyaluronate binding domain of CD44 antigen monomer, 18 kDa Homo sapiens protein
Single-chain Variable Fragment of Antibody MEM-85 monomer, 29 kDa Mus musculus protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
Molecular mechanism for the action of the anti-CD44 monoclonal antibody MEM-85. J Struct Biol 191(2):214-23 (2015)
Škerlová J, Král V, Kachala M, Fábry M, Bumba L, Svergun DI, Tošner Z, Veverka V, Řezáčová P
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 57 nm3