Browse by ORGANISM: Homo sapiens (Human)

SASDAZ4 – fH1114

Factor H CCP modules 11 to 14 experimental SAS data
DAMMIF model
Sample: Factor H CCP modules 11 to 14 monomer, 28 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 10.5 nm
VolumePorod 38 nm3

SASDA25 – fh1213

Factor H CCP modules 12 to 13 experimental SAS data
CRYSOL model
Sample: Factor H CCP modules 12 to 13 monomer, 14 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 2.0 nm
Dmax 7.1 nm
VolumePorod 20 nm3

SASDHE2 – Type 1 insulin-like growth factor receptor ectodomains (IGF-1RΔβ)

Insulin-like growth factor 1 receptor experimental SAS data
BUNCH model
Sample: Insulin-like growth factor 1 receptor dimer, 202 kDa Homo sapiens protein
Buffer: 30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Apr 22
Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformational change. J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC
RgGuinier 5.1 nm
Dmax 16.0 nm
VolumePorod 357 nm3

SASDHF2 – Insulin receptor ectodomains (IRΔβ)

Insulin receptor experimental SAS data
BUNCH model
Sample: Insulin receptor dimer, 203 kDa Homo sapiens protein
Buffer: 30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Dec 7
Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformational change. J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC
RgGuinier 5.5 nm
Dmax 17.0 nm
VolumePorod 385 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 EMBL X33, DORIS III, DESY 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 EMBL X33, DORIS III, DESY 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

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 EMBL X33, DORIS III, DESY 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

SASDAQ4 – 6:3 complex of GAD:CaM

CalmodulinGlutamate decarboxylase experimental SAS data
BUNCH model
Sample: Calmodulin monomer, 17 kDa Homo sapiens protein
Glutamate decarboxylase hexamer, 340 kDa Petunia x hybrida protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 Nov 9
A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase. J Mol Biol 392(2):334-51 (2009)
Gut H, Dominici P, Pilati S, Astegno A, Petoukhov MV, Svergun DI, Grütter MG, Capitani G
RgGuinier 5.9 nm
Dmax 23.0 nm
VolumePorod 630 nm3

SASDN33 – Ternary Human Pex5p(C-terminal)-Pex14p(N)-PTS1 Complex (1:1:1 stoichiometry)

Peroxisomal targeting signal 1 receptor (C -terminal)Peroxisomal membrane protein PEX14 (N-terminal)PTS1-BP experimental SAS data
DAMMIN model
Sample: Peroxisomal targeting signal 1 receptor (C -terminal) monomer, 48 kDa Homo sapiens protein
Peroxisomal membrane protein PEX14 (N-terminal) monomer, 7 kDa Homo sapiens protein
PTS1-BP monomer, 14 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Oct 3
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 110 nm3

SASDN43 – Full-length Human Pex5p protein

Peroxisomal targeting signal 1 receptor experimental SAS data
DAMMIN model
Sample: Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Buffer: 50 mM HEPES-KOH (pH 7.5), 100mM KCl, and 20mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 24
Solution structure of human Pex5.Pex14.PTS1 protein complexes obtained by small angle X-ray scattering. J Biol Chem 284(37):25334-42 (2009)
Shiozawa K, Konarev PV, Neufeld C, Wilmanns M, Svergun DI
RgGuinier 5.0 nm
Dmax 20.0 nm
VolumePorod 181 nm3