Browse by MACROMOLECULE type: protein

SASDAS3 – Fila16-17

immunoglobulin- like filamin two-domain fragment 16-17 experimental SAS data
GASBOR model
Sample: Immunoglobulin- like filamin two-domain fragment 16-17 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 33 nm3

SASDAT3 – Fila18-19

immunoglobulin- like filamin two-domain fragment 18-19 experimental SAS data
GASBOR model
Sample: Immunoglobulin- like filamin two-domain fragment 18-19 monomer, 20 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 34 nm3

SASDAU3 – Fila22-23

immunoglobulin- like filamin two-domain fragment 22-23 experimental SAS data
GASBOR model
Sample: Immunoglobulin- like filamin two-domain fragment 22-23 monomer, 19 kDa Escherichia coli protein
Buffer: 100 mM NaCl 10 mM dithiothreitol 20 mM Tris, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 18
Atomic structures of two novel immunoglobulin-like domain pairs in the actin cross-linking protein filamin. J Biol Chem 284(37):25450-8 (2009)
Heikkinen OK, Ruskamo S, Konarev PV, Svergun DI, Iivanainen T, Heikkinen SM, Permi P, Koskela H, Kilpeläinen I, Ylänne J
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 32 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

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