Browse by ORGANISM: Homo sapiens (Human)

SASDLV5 – Myosin Filament-Linking Protein Myomesin-1 (domains My9-My13, dimer)

Myomesin-1 experimental SAS data
DAMMIN model
Sample: Myomesin-1 dimer, 121 kDa Homo sapiens protein
Buffer: 25 mMTris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 May 10
Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties. PLoS Biol 10(2):e1001261 (2012)
Pinotsis N, Chatziefthimiou SD, Berkemeier F, Beuron F, Mavridis IM, Konarev PV, Svergun DI, Morris E, Rief M, Wilmanns M
RgGuinier 9.6 nm
Dmax 37.0 nm

SASDHZ2 – 14-3-3 protein beta isoform

14-3-3 protein beta/alpha experimental SAS data
BUNCH model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 92 nm3

SASDH33 – Rho GTPase-activating protein 22

Rho GTPase-activating protein 22 experimental SAS data
BUNCH model
Sample: Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 88 nm3

SASDH83 – Chemically crossed linked complex between Rho GTPase-activating protein 22 (ARHGAP22) and the beta isoform of the 14-3-3 protein beta/alpha

14-3-3 protein beta/alphaRho GTPase-activating protein 22 experimental SAS data
CORAL model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 195 nm3

SASDAS6 – Plectin, fragment of the plakin domain encompassing the spectrin repeats SR3-SR4-SR5 and the SH3

Plectin experimental SAS data
DAMMIF model
Sample: Plectin monomer, 43 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 2.5 mM DTT, pH: 7.5
Experiment: SAXS data collected at cSAXS, Swiss Light Source on 2009 Jul 24
The structure of the plakin domain of plectin reveals a non-canonical SH3 domain interacting with its fourth spectrin repeat. J Biol Chem 286(14):12429-38 (2011)
Ortega E, Buey RM, Sonnenberg A, de Pereda JM
RgGuinier 4.4 nm
Dmax 14.5 nm
VolumePorod 57 nm3

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 EMBL X33, DORIS III, DESY 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

SASDMN9 – Conformational characterization of A77-78 fibronectin type III tandem

Titin experimental SAS data
OTHER model
Sample: Titin monomer, 22 kDa Homo sapiens protein
Buffer: 100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jul 3
The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin Journal of Molecular Biology 401(5):843-853 (2010)
Bucher R, Svergun D, Muhle-Goll C, Mayans O
RgGuinier 2.5 nm
Dmax 90.0 nm
VolumePorod 21 nm3

SASDMP9 – Conformational characterization of A80-82 fibronectin type III tandem

Titin experimental SAS data
SASREF model
Sample: Titin monomer, 32 kDa Homo sapiens protein
Buffer: 100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jul 3
The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin Journal of Molecular Biology 401(5):843-853 (2010)
Bucher R, Svergun D, Muhle-Goll C, Mayans O
RgGuinier 3.7 nm
Dmax 130.0 nm
VolumePorod 39 nm3

SASDMQ9 – Conformational characterization of A84-86 fibronectin type III tandem

Titin experimental SAS data
SASREF model
Sample: Titin monomer, 32 kDa Homo sapiens protein
Buffer: 100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 6
The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin Journal of Molecular Biology 401(5):843-853 (2010)
Bucher R, Svergun D, Muhle-Goll C, Mayans O
RgGuinier 3.7 nm
Dmax 14.0 nm

SASDAY4 – fH1015

Factor H CCP modules 10 to 15 experimental SAS data
DAMMIF model
Sample: Factor H CCP modules 10 to 15 monomer, 41 kDa Homo sapiens protein
Buffer: 50 mM Potassium Phosphate, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Dec 2
The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module. J Mol Biol 395(1):105-22 (2010)
Schmidt CQ, Herbert AP, Mertens HD, Guariento M, Soares DC, Uhrin D, Rowe AJ, Svergun DI, Barlow PN
RgGuinier 3.0 nm
Dmax 10.4 nm
VolumePorod 68 nm3