Browse by MACROMOLECULE type: protein

SASDE29 – Interleukin-1 receptor accessory protein ectodomain with RI linker

Interleukin-1 receptor accessory protein ectodomain with RI linker experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor accessory protein ectodomain with RI linker monomer, 41 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Aug 11
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.0 nm
Dmax 10.4 nm
VolumePorod 76 nm3

SASDE39 – Interleukin-18 receptor accessory protein ectodomain with Rα linker

Interleukin-18 receptor accessory protein ectodomain with Rα linker experimental SAS data
BILBOMD model
Sample: Interleukin-18 receptor accessory protein ectodomain with Rα linker monomer, 41 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jul 24
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.4 nm
Dmax 11.5 nm
VolumePorod 72 nm3

SASDE49 – Interleukin-1 receptor accessory protein ectodomains with ST2 linker

Interleukin-1 receptor accessory protein ectodomains with ST2 linker experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor accessory protein ectodomains with ST2 linker monomer, 41 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jul 24
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.1 nm
Dmax 10.7 nm
VolumePorod 76 nm3

SASDE59 – Interleukin-1 receptor type 1, IL-1RI-ECD

Interleukin-1 receptor type 1 experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor type 1 monomer, 37 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jul 22
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 63 nm3

SASDE69 – Interleukin-1 receptor type 2, IL-1RII-ECD

Interleukin-1 receptor type 2 experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor type 2 monomer, 38 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jul 24
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 2.8 nm
Dmax 9.9 nm
VolumePorod 80 nm3

SASDE79 – Interleukin-18 receptor 1, IL-18Rα-ECD

Interleukin-18 receptor 1 experimental SAS data
BILBOMD model
Sample: Interleukin-18 receptor 1 monomer, 36 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Oct 3
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.1 nm
Dmax 10.9 nm
VolumePorod 77 nm3

SASDE89 – Interleukin-1 receptor accessory protein ectodomain with RII linker

Interleukin-1 receptor accessory protein ectodomains with RII linker experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor accessory protein ectodomains with RII linker monomer, 41 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jul 24
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.0 nm
Dmax 10.7 nm
VolumePorod 75 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 protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae 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
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
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 protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae 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
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
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 protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae 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
Histone chaperone exploits intrinsic disorder to switch acetylation specificity. Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.3 nm
Dmax 10.5 nm