SASDA65 – Nucleoplasmin-H5 complex

NP-H5 experimental SAS data
MONSA model
Sample: NP-H5 pentamer, 200 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2007 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 5.2 nm
Dmax 16.7 nm
VolumePorod 410 nm3

SASDA75 – Nucleoplasmin-H2AH2B complex

NP-H2AH2B experimental SAS data
MONSA model
Sample: NP-H2AH2B pentamer, 250 kDa Escherichia coli protein
Buffer: 20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2014 Dec 3
A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA
RgGuinier 4.7 nm
Dmax 14.5 nm
VolumePorod 470 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 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 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

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 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 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 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

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

1719 hits found.