Browse by MODEL: No model

SASDAF8 – Human Filamin A Ig-like domains 20-21 truncation (2151-2329)

Human Filamin A Ig-like domains 20-21 experimental SAS data
Human Filamin A Ig-like domains 20-21 Kratky plot
Sample: Human Filamin A Ig-like domains 20-21 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 29 nm3

SASDAG8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329) in complex with migfilin peptide

Human Filamin A Ig-like domains 20-21*/migfilin peptide complex experimental SAS data
Human Filamin A Ig-like domains 20-21*/migfilin peptide complex Kratky plot
Sample: Human Filamin A Ig-like domains 20-21*/migfilin peptide complex monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
Flexible Structure of Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 33 nm3

SASDBH6 – Full-length human p23 (1-160)

Prostaglandin E synthase 3 experimental SAS data
Prostaglandin E synthase 3 Kratky plot
Sample: Prostaglandin E synthase 3 monomer, 19 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 2.5 nm
Dmax 10.0 nm
VolumePorod 40 nm3

SASDBJ6 – Truncated construct of human p23 (1-142)

Prostaglandin E synthase 3 (1-142) experimental SAS data
Prostaglandin E synthase 3 (1-142) Kratky plot
Sample: Prostaglandin E synthase 3 (1-142) monomer, 17 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 2.1 nm
Dmax 8.5 nm
VolumePorod 36 nm3

SASDBK6 – Truncated construct of human p23 (1-131)

Prostaglandin E synthase 3 (1-131) experimental SAS data
Prostaglandin E synthase 3 (1-131) Kratky plot
Sample: Prostaglandin E synthase 3 (1-131) monomer, 16 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 31 nm3

SASDBL6 – Truncated construct of human p23 (1-117)

Prostaglandin E synthase 3 (1-117) experimental SAS data
Prostaglandin E synthase 3 (1-117) Kratky plot
Sample: Prostaglandin E synthase 3 (1-117) monomer, 14 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2013 Jun 21
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 29 nm3

SASDA76 – NetrinVIV DCC56 complex

Netrin-1Deleted in Colorectal Cancer (FN5 & FN6) experimental SAS data
Netrin-1 Deleted in Colorectal Cancer (FN5 & FN6) Kratky plot
Sample: Netrin-1 monomer, 49 kDa Homo sapiens protein
Deleted in Colorectal Cancer (FN5 & FN6) monomer, 26 kDa Homo sapiens protein
Buffer: 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Oct 31
The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83(4):839-849 (2014)
Finci LI, Krüger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R
RgGuinier 5.1 nm
Dmax 17.0 nm
VolumePorod 120 nm3

SASDA86 – NetrinVIV DCC56(M933R) complex

Netrin-1Deleted in Colorectal Cancer (FN5 & FN6) M933R mutant experimental SAS data
Netrin-1 Deleted in Colorectal Cancer (FN5 & FN6) M933R mutant Kratky plot
Sample: Netrin-1 monomer, 49 kDa Homo sapiens protein
Deleted in Colorectal Cancer (FN5 & FN6) M933R mutant monomer, 26 kDa Homo sapiens protein
Buffer: 25 MES mM 200 mM NaCl 50 mM Tris 0.2 M ammonium sulfate (NH4)2(SO4) 1mM calcium chloride CaCl2, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 26
The crystal structure of netrin-1 in complex with DCC reveals the bifunctionality of netrin-1 as a guidance cue. Neuron 83(4):839-849 (2014)
Finci LI, Krüger N, Sun X, Zhang J, Chegkazi M, Wu Y, Schenk G, Mertens HDT, Svergun DI, Zhang Y, Wang JH, Meijers R
RgGuinier 4.0 nm
Dmax 14.0 nm
VolumePorod 95 nm3

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.5 nm
Dmax 29.0 nm
VolumePorod 750 nm3

SASDAY3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.3 nm
Dmax 29.0 nm
VolumePorod 720 nm3