Browse by MACROMOLECULE type: protein

SASDC42 – Ethylene Receptor 1 Cytosolic Domain

Ethylene Receptor 1 experimental SAS data
Ethylene Receptor 1 Cytosolic Domain Rg histogram
Sample: Ethylene Receptor 1 dimer, 129 kDa Arabidopsis thaliana protein
Buffer: 20 mM TRIS 150 mM NaCl 1mM DTT 250mM NDSB, pH: 8.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Mar 29
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 5.5 nm
Dmax 19.0 nm
VolumePorod 274 nm3

SASDC97 – Ethylene Receptor 1 (DHp + CA + RD domains)

Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains experimental SAS data
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains Kratky plot
Sample: Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains dimer, 88 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM DTT 5 mM ADP, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 11
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 4.0 nm
Dmax 13.9 nm
VolumePorod 144 nm3

SASDCA7 – Ethylene Receptor 1 (DHp + CA domains)

Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains experimental SAS data
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains Kratky plot
Sample: Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains dimer, 55 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM DTT 5 mM ADP, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 11
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 2.7 nm
Dmax 8.7 nm
VolumePorod 74 nm3

SASDL57 – Thermus thermophilus 3-isopropylmalate dehydrogenase

3-isopropylmalate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3-isopropylmalate dehydrogenase dimer, 73 kDa Thermus thermophilus protein
Buffer: 25 mM MOPS/NaOH, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 3
Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase. FEBS Lett 589(2):240-5 (2015)
Gráczer É, Palló A, Oláh J, Szimler T, Konarev PV, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M
RgGuinier 2.8 nm

SASDA46 – TIP5 in Tris

Bromodomain adjacent to zinc finger domain protein 2A experimental SAS data
BUNCH model
Sample: Bromodomain adjacent to zinc finger domain protein 2A monomer, 27 kDa Homo sapiens protein
Buffer: 20 mM Tris 500 mM NaCl 2 mM DTT 10 microM ZnCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Mar 16
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Structure 23(1):80-92 (2015)
Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 45 nm3

SASDA56 – BAZ2B in Tris

Bromodomain adjacent to zinc finger domain protein 2B, C-terminal experimental SAS data
EOM/RANCH model
Sample: Bromodomain adjacent to zinc finger domain protein 2B, C-terminal monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Tris 500 mM NaCl 2 mM DTT 10 microM ZnCl2, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 24
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Structure 23(1):80-92 (2015)
Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A
RgGuinier 4.0 nm
Dmax 14.5 nm
VolumePorod 43 nm3

SASDA66 – BAZ2B-18mer complex in Tris

Bromodomain adjacent to zinc finger domain protein 2B, C-terminalH3Kac9Kac14 experimental SAS data
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 Kratky plot
Sample: Bromodomain adjacent to zinc finger domain protein 2B, C-terminal monomer, 28 kDa Homo sapiens protein
H3Kac9Kac14 monomer, 5 kDa Homo sapiens protein
Buffer: 20 mM Tris 500 mM NaCl 2 mM DTT 10 microM ZnCl2, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Sep 24
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Structure 23(1):80-92 (2015)
Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A
RgGuinier 4.2 nm
Dmax 16.0 nm
VolumePorod 52 nm3

SASDAH6 – WbdD(1-459)

bifunctional kinase- methyltransferase WbdD experimental SAS data
CORAL model
Sample: Bifunctional kinase- methyltransferase WbdD monomer, 59 kDa Escherichia coli protein
Buffer: 20 mM BisTris 50 mM NaCl 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Sep 23
A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide. Nat Struct Mol Biol 22(1):50-56 (2015)
Hagelueken G, Clarke BR, Huang H, Tuukkanen A, Danciu I, Svergun DI, Hussain R, Liu H, Whitfield C, Naismith JH
RgGuinier 3.1 nm
Dmax 10.0 nm
VolumePorod 90 nm3

SASDAJ6 – WbdD(1-556)

bifunctional kinase- methyltransferase WbdD experimental SAS data
CORAL model
Sample: Bifunctional kinase- methyltransferase WbdD trimer, 190 kDa protein
Buffer: 20 mM BisTris 50 mM NaCl 5 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 2
A coiled-coil domain acts as a molecular ruler to regulate O-antigen chain length in lipopolysaccharide. Nat Struct Mol Biol 22(1):50-56 (2015)
Hagelueken G, Clarke BR, Huang H, Tuukkanen A, Danciu I, Svergun DI, Hussain R, Liu H, Whitfield C, Naismith JH
RgGuinier 5.2 nm
Dmax 17.0 nm
VolumePorod 380 nm3

SASDAE8 – Human Filamin A Ig-like domains 20-21 truncation (2151-2329) 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, 21 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 31 nm3