Browse by MACROMOLECULE type: protein

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

SASDN53 – Ternary Human Pex5p(full-length)-Pex14p(N)-PTS1 Protein Complex (1:7:1 stoichiometry)

Peroxisomal targeting signal 1 receptorPeroxisomal membrane protein PEX14PTS1-BP experimental SAS data
SASREF model
Sample: Peroxisomal targeting signal 1 receptor monomer, 71 kDa Homo sapiens protein
Peroxisomal membrane protein PEX14 monomer, 7 kDa Homo sapiens protein
PTS1-BP monomer, 13 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 Mar 18
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 6.0 nm
Dmax 20.0 nm
VolumePorod 267 nm3

SASDH62 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 7
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 123 nm3

SASDH72 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 8
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 151 nm3

SASDH82 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08

Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 11
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.6 nm
Dmax 11.4 nm
VolumePorod 145 nm3

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 EMBL X33, DORIS III, DESY 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

SASDAR5 – ProNGF

ProNGF experimental SAS data
DAMMIN model
Sample: ProNGF dimer, 45 kDa Mouse submandibulary glands protein
Buffer: 50 mM Naphosphat 0.5 M Ammonium Sulfate(NH4)2SO4, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 25
Intrinsic structural disorder of mouse proNGF. Proteins 75(4):990-1009 (2009)
Paoletti F, Covaceuszach S, Konarev PV, Gonfloni S, Malerba F, Schwarz E, Svergun DI, Cattaneo A, Lamba D
RgGuinier 2.6 nm
Dmax 8.0 nm
VolumePorod 92 nm3

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 EMBL X33, DORIS III, DESY 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

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 EMBL X33, DORIS III, DESY 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

SASDMC7 – Nuclear fragile X mental retardation-interacting protein 2 (FRMP)

Nuclear fragile X mental retardation-interacting protein 2 experimental SAS data
DAMMIN model
Sample: Nuclear fragile X mental retardation-interacting protein 2 monomer, 59 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl pH 8.0, 5 mM TCEP, pH:
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 11
A study of the ultrastructure of fragile-X-related proteins. Biochem J 419(2):347-57 (2009)
Sjekloća L, Konarev PV, Eccleston J, Taylor IA, Svergun DI, Pastore A
RgGuinier 4.1 nm
Dmax 15.0 nm
VolumePorod 92 nm3