Advanced search

  • Select one or multiple fields to restrict your search.
    If none is selected the search will be in every field.
 

9 hits found for KWS1

SASDDZ5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states IUCrJ 5(6) (2018)
Larsen A, Dorosz J, Thorsen T, Johansen N, Darwish T, Midtgaard S, Arleth L, Kastrup J
RgGuinier 6.3 nm
Dmax 18.4 nm
VolumePorod 407 nm3

SASDD26 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 5.5

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 10 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 5.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states IUCrJ 5(6) (2018)
Larsen A, Dorosz J, Thorsen T, Johansen N, Darwish T, Midtgaard S, Arleth L, Kastrup J
RgGuinier 6.5 nm
Dmax 18.9 nm
VolumePorod 899 nm3

SASDD36 – AMPA subtype ionotropic Glutamate receptor GluA2 in the GYKI-53655 bound state, in stealth DDM detergents

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM GYKI-53655, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states IUCrJ 5(6) (2018)
Larsen A, Dorosz J, Thorsen T, Johansen N, Darwish T, Midtgaard S, Arleth L, Kastrup J
RgGuinier 6.3 nm
Dmax 18.6 nm
VolumePorod 384 nm3

SASDFL3 – All 1H histone acetyltransferase Rtt109 complex with histones H3 and H4 and histone chaperones Asf1 and Vps75 (acquired in 100% v/v D2O)

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae (strain ... protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae (strain ... protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 3
Asf1-H3:H4-Rtt109-Vps75 protein complex
Nataliya Danilenko
RgGuinier 3.5 nm
Dmax 11.8 nm

SASDFM3 – Complex with 1H histone chaperone Asf1 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1H Asf1-H3:H4, 2H Rtt109-Vps75) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae (strain ... protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae (strain ... protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
Asf1-H3:H4-Rtt109-Vps75 protein complex
Nataliya Danilenko
RgGuinier -2.8 nm

SASDFN3 – Complex with 1H histone chaperones Asf1 and Vps75 and histones H3 and H4, 70%-2H histone acetyltransferase Rtt109 (1H Asf1-H3:H4-Vps75, 2H(70%) Rtt109) acquired in 100% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae (strain ... protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae (strain ... protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 4
Asf1-H3:H4-Rtt109-Vps75 protein complex
Nataliya Danilenko
RgGuinier 3.3 nm
Dmax 10.5 nm

SASDFQ3 – Complex with 1H histone acetyltransferase Rtt109 and histones H3 and H4, 2H histone chaperones Asf1 and Vps75 (1H Rtt109-H3:H4, 2H Asf1-Vps75) acquired in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae (strain ... protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae (strain ... protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
Asf1-H3:H4-Rtt109-Vps75 protein complex
Nataliya Danilenko
RgGuinier 3.5 nm
Dmax 11.0 nm

SASDFR3 – Complex with 1H histone chaperone Vps75 and histones H3 and H4, 2H histone acetyltransferase Rtt109 and histone chaperone Asf1 (1H Vps75-H3:H4, 2H Rtt109-Asf1) acquired in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H3.2 (35-135 aa)Histone H4 experimental SAS data
HADDOCK model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae (strain ... protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae (strain ... protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H3.2 (35-135 aa) monomer, 12 kDa Xenopus laevis protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Mar 5
Asf1-H3:H4-Rtt109-Vps75 protein complex
Nataliya Danilenko
RgGuinier 3.1 nm
Dmax 10.5 nm

SASDDY5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states IUCrJ 5(6) (2018)
Larsen A, Dorosz J, Thorsen T, Johansen N, Darwish T, Midtgaard S, Arleth L, Kastrup J
RgGuinier 6.0 nm
Dmax 17.9 nm
VolumePorod 396 nm3