10 hits found for Vacuolar protein sorting-associated protein 75 (1-225 aa)

SASDFL3 – ...75 (acquired in 100% v/v D2O) 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 ...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 – ...75 (1H Asf1-H3:H4, 2H Rtt109-Vps75) acquired in 100% v/v D2O 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 ...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 – ...75 and histones H3 and H4, 70%-2H histone acetyltransferase Rtt109 (1H Asf1-H3:H4-Vps75, 2H(70%) Rtt109) acquired in 100% v/v D2O 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 ...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

SASDFP3 – ...75 (1H Asf1-H3:H4-Rtt109, 2H(70%) Vps75) acquired in 100% v/v D2O 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 ...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 D22, Institut Laue-Langevin (ILL) on 2018 May 29 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 Dmax 9.5 nm

SASDFQ3 – ...75 (1H Rtt109-H3:H4, 2H Asf1-Vps75) acquired in 42% v/v D2O 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 ...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 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 11.0 nm

SASDFR3 – ...75 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 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 ...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 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 3.1 nm Dmax 10.5 nm

SASDFK7 – ...aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O 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 ...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 D22, Institut Laue-Langevin (ILL) on 2016 Nov 14 ...75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019) Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T RgGuinier 1.9 nm Dmax 5.5 nm

SASDFL7 – ...75 (1-225aa) in 42% v/v D2O 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 H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14 ...75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019) Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T RgGuinier 3.4 nm Dmax 10.5 nm

SASDFM7 – ...75 (1-225aa) in 42% v/v D2O 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 H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14 ...75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019) Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T RgGuinier 2.7 nm Dmax 9.0 nm

SASDFN7 – ...75 (1-225aa) (acquired in 100% v/v D2O) 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 H4 monomer, 11 kDa Xenopus laevis protein Histone H3 full-length monomer, 15 kDa Xenopus laevis protein Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O, pH: 6.5 Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 May 30 ...75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019) Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T RgGuinier 3.5 nm Dmax 11.0 nm