Browse by MACROMOLECULE type: protein

SASDLR3 – Interleukin 11 Mutein

Interleukin 11 Mutein experimental SAS data
OTHER model
Sample: Interleukin 11 Mutein 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
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 1.8 nm
Dmax 5.4 nm
VolumePorod 25 nm3

SASDLS3 – Interleukin 11 Mutein, complex with gp130 (domains 1-3) and IL-11Rα

Interleukin-11 receptor subunit alphaInterleukin 11 MuteinInterleukin-6 receptor subunit beta experimental SAS data
DAMMIN model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Interleukin 11 Mutein monomer, 18 kDa Homo sapiens protein
Interleukin-6 receptor subunit beta monomer, 35 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
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 4.4 nm
Dmax 15.6 nm
VolumePorod 160 nm3

SASDRB8 – Human tRNA guanine transglycosylase heterodimer

Queuine tRNA-ribosyltransferase catalytic subunit 1Queuine tRNA-ribosyltransferase accessory subunit 2 experimental SAS data
Human tRNA guanine transglycosylase heterodimer Rg histogram
Sample: Queuine tRNA-ribosyltransferase catalytic subunit 1 monomer, 44 kDa Homo sapiens protein
Queuine tRNA-ribosyltransferase accessory subunit 2 monomer, 47 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 100 mM NaCl, 3% (w/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2022 Dec 1
Structural and functional investigation of tRNA guanine transglycosylase University of Göttingen Dissertation - (2023)
Katharina Sievers
RgGuinier 3.3 nm
Dmax 11.4 nm
VolumePorod 127 nm3

SASDNW6 – AIP56, an AB-toxin from Photobacterium damselae subsp. piscicida

Apoptosis inducing protein experimental SAS data
OTHER model
Sample: Apoptosis inducing protein monomer, 57 kDa Photobacterium damselae subsp. … protein
Buffer: 50 mM Hepes, 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Apr 13
Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56. Nat Commun 14(1):7431 (2023)
Lisboa J, Pereira C, Pinto RD, Rodrigues IS, Pereira LMG, Pinheiro B, Oliveira P, Pereira PJB, Azevedo JE, Durand D, Benz R, do Vale A, Dos Santos NMS
RgGuinier 2.8 nm
Dmax 9.5 nm
VolumePorod 76 nm3

SASDSJ2 – Ribosome maturation factor RimP bound to 30S ribosomal protein S12 (RimP-uS12 complex from Staphylococcus aureus)

Ribosome maturation factor RimP30S ribosomal protein S12 experimental SAS data
DAMMIN model
Sample: Ribosome maturation factor RimP monomer, 18 kDa Staphylococcus aureus (strain … protein
30S ribosomal protein S12 monomer, 15 kDa Staphylococcus aureus (strain … protein
Buffer: 50 mM sodium phosphate, 200 mM NaCl, pH: 7
Experiment: SAXS data collected at Xeuss 3.0 SAXS/WAXS System, JINR on 2023 Feb 16
Structural aspects of RimP binding on small ribosomal subunit from Staphylococcus aureus. Structure (2023)
Garaeva N, Fatkhullin B, Murzakhanov F, Gafurov M, Golubev A, Bikmullin A, Glazyrin M, Kieffer B, Jenner L, Klochkov V, Aganov A, Rogachev A, Ivankov O, Validov S, Yusupov M, Usachev K
RgGuinier 2.4 nm
Dmax 10.0 nm
VolumePorod 39 nm3

SASDM79 – Lysozyme crystallization solutions with precipitants from crystallization kits CS 1 and CS2 (mixture of monomers, dimers and octamers, with octamer volume fractions from 0 to 0.7%)

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 100 mM HEPES pH 7.5, 20 %(v/v) jeffamine M-600, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 28
Dependence of concentration of precursor clusters formed in lysozyme crystallization solutions on degree of supersaturation and its effect on character of solution transition from liquid to condensed phase
Petr Konarev
RgGuinier 1.8 nm

SASDM89 – Lysozyme crystallization solutions with precipitants from crystallization kits CS 1 and CS2 (mixture of monomers, dimers and octamers, with octamer volume fractions from 0.9% to 4.4%)

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 100 mM sodium acetate, pH 4.6, 2.0 M sodium formate, pH: 4.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 28
Dependence of concentration of precursor clusters formed in lysozyme crystallization solutions on degree of supersaturation and its effect on character of solution transition from liquid to condensed phase
Petr Konarev
RgGuinier 2.2 nm

SASDM99 – Lysozyme crystallization solutions with precipitants from crystallization kits CS 1 and CS2 (mixture of monomers, dimers and octamers, with octamer volume fractions from 4.9% to 21.1%)

Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 200 mM K/Na tartrate, 100 mM tri-sodium citrate pH 5.6, 2.0 M ammonium sulfate, pH: 5.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Aug 28
Dependence of concentration of precursor clusters formed in lysozyme crystallization solutions on degree of supersaturation and its effect on character of solution transition from liquid to condensed phase
Petr Konarev
RgGuinier 2.4 nm

SASDQ97 – Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E]

DNA repair protein RAD51 homolog 1 (F86E A89E) experimental SAS data
Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] Rg histogram
Sample: DNA repair protein RAD51 homolog 1 (F86E A89E) monomer, 37 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 200 mM Na2SO4, 5% glycerol, 0.1 mM EDTA, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Apr 7
Isolation and characterization of monomeric human RAD51: a novel tool for investigating homologous recombination in cancer Angewandte Chemie International Edition (2023)
Rinaldi F, Schipani F, Balboni B, Catalano F, Marotta R, Myers S, Previtali V, Veronesi M, Scietti L, Cecatiello V, Pasqualato S, Ortega J, Girotto S, Cavalli A
RgGuinier 3.0 nm
Dmax 14.2 nm
VolumePorod 61 nm3

SASDQT9 – Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with fourth BRC repeat (BRC4)

DNA repair protein RAD51 homolog 1 (F86E A89E)Breast cancer type 2 susceptibility protein experimental SAS data
Monomeric DNA repair protein RAD51 homolog 1 double mutant [F86E, A89E] in complex with fourth BRC repeat (BRC4) Rg histogram
Sample: DNA repair protein RAD51 homolog 1 (F86E A89E) monomer, 37 kDa Homo sapiens protein
Breast cancer type 2 susceptibility protein monomer, 4 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 50 mM Na2SO4, 2% v/v sucrose, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Dec 7
Isolation and characterization of monomeric human RAD51: a novel tool for investigating homologous recombination in cancer Angewandte Chemie International Edition (2023)
Rinaldi F, Schipani F, Balboni B, Catalano F, Marotta R, Myers S, Previtali V, Veronesi M, Scietti L, Cecatiello V, Pasqualato S, Ortega J, Girotto S, Cavalli A
RgGuinier 2.9 nm
Dmax 15.6 nm
VolumePorod 70 nm3