Browse by MACROMOLECULE type: protein

SASDGG2 – Interleukin 11 receptor subunit alpha

Interleukin-11 receptor subunit alpha experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement Journal of Biological Chemistry :jbc.RA119.012351 (2020)
Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 3.0 nm
Dmax 9.5 nm
VolumePorod 41 nm3

SASDGH2 – Interleukin 11, N-terminally truncated

Interleukin 11 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Interleukin 11 monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement Journal of Biological Chemistry :jbc.RA119.012351 (2020)
Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 1.7 nm
Dmax 5.4 nm
VolumePorod 22 nm3

SASDGJ2 – Interleukin 11, full length

Interleukin 11 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Interleukin 11 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement Journal of Biological Chemistry :jbc.RA119.012351 (2020)
Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 1.9 nm
Dmax 6.1 nm
VolumePorod 28 nm3

SASDGK2 – Interleukin 11/Interleukin 11 receptor alpha complex

Interleukin-11 receptor subunit alphaInterleukin 11 experimental SAS data
OTHER model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Interleukin 11 monomer, 18 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
The structure of the extracellular domains of human interleukin 11 α-receptor reveals mechanisms of cytokine engagement Journal of Biological Chemistry :jbc.RA119.012351 (2020)
Metcalfe R, Aizel K, Zlatic C, Nguyen P, Morton C, Lio D, Cheng H, Dobson R, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 3.3 nm
Dmax 10.2 nm
VolumePorod 84 nm3

SASDHR9 – GntR-type transcriptional regulator NanR from Escherichia coli

HTH-type transcriptional repressor NanR experimental SAS data
CUSTOM IN-HOUSE model
Sample: HTH-type transcriptional repressor NanR dimer, 59 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1 % (w/v) sodium azide, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Apr 20
Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism (2020)
Horne C, Venugopal H, Panjikar S, Henrickson A, Brookes E, North R, Murphy J, Friemann R, Griffin M, Ramm G, Demeler B, Dobson R
RgGuinier 3.2 nm
Dmax 10.5 nm
VolumePorod 110 nm3

SASDHS9 – GntR-type transcriptional regulator NanR from Escherichia coli in the presence of N-acetylneuraminic acid

HTH-type transcriptional repressor NanR experimental SAS data
CUSTOM IN-HOUSE model
Sample: HTH-type transcriptional repressor NanR dimer, 59 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 20 mM Neu5Ac and 0.1 % (w/v) sodium azide, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Apr 20
Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism (2020)
Horne C, Venugopal H, Panjikar S, Henrickson A, Brookes E, North R, Murphy J, Friemann R, Griffin M, Ramm G, Demeler B, Dobson R
RgGuinier 3.1 nm
Dmax 10.1 nm
VolumePorod 105 nm3

SASDFV6 – DNA-binding protein HU-alpha, E38K/V42L double mutant

DNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha, E38K/V42L double mutant decamer, 95 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 53 nm3

SASDHT4 – Phosphoprotein from Nipah virus

Phosphoprotein experimental SAS data
Phosphoprotein Kratky plot
Sample: Phosphoprotein tetramer, 317 kDa Nipah henipavirus protein
Buffer: 20 mM Tris-HCL, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 3
Structural Description of the Nipah Virus Phosphoprotein and Its Interaction with STAT1. Biophys J (2020)
Jensen MR, Yabukarski F, Communie G, Condamine E, Mas C, Volchkova V, Tarbouriech N, Bourhis JM, Volchkov V, Blackledge M, Jamin M
RgGuinier 10.9 nm
Dmax 39.3 nm

SASDHQ5 – Ile-Leu-Gln-Ile-Asn-Ser (ILQINS) hexapeptide self-assembly

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
OTHER model
Sample: Ile-Leu-Gln-Ile-Asn-Ser peptide, 1 kDa synthetic construct protein
Buffer: pure (MQ, 18 MΩ) Water, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 1
Amyloid Evolution: Antiparallel Replaced by Parallel. Biophys J (2020)
Zanjani AAH, Reynolds NP, Zhang A, Schilling T, Mezzenga R, Berryman JT

SASDHK8 – Ile-Leu-Gln-Ile-Asn-Ser (ILQINS) hexapeptide self-assembly (2019-dataset)

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
Ile-Leu-Gln-Ile-Asn-Ser peptide Kratky plot
Sample: Ile-Leu-Gln-Ile-Asn-Ser peptide, 1 kDa synthetic construct protein
Buffer: pure (MQ, 18 MΩ) Water, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 1
Amyloid Evolution: Antiparallel Replaced by Parallel. Biophys J (2020)
Zanjani AAH, Reynolds NP, Zhang A, Schilling T, Mezzenga R, Berryman JT