Small Angle Scattering Biological Data Bank SASBDB


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7 hits found for Histone H3.2 (35-135 aa)

SASDFL3 – ...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

Sample:	...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

R_g^Guinier	3.5	nm
D_max	11.8	nm

SASDFM3 – ...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

Sample:	...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

R_g^Guinier

-2.8

SASDFN3 – ...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

Sample:	...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

R_g^Guinier	3.3	nm
D_max	10.5	nm

SASDFP3 – ...histone chaperone Asf1, acetyltransferase Rtt109 and histones H3 and H4, 70%-2H histone chaperone Vps75 (1H Asf1-H3:H4-Rtt109, 2H(70%) Vps75) acquired in 100% v/v D2O

Sample:	...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 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

R_g^Guinier	2.8	nm
D_max	9.5	nm

SASDFQ3 – ...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

Sample:	...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, 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

R_g^Guinier	3.5	nm
D_max	11.0	nm

SASDFR3 – ...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

Sample:	...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, 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

R_g^Guinier	3.1	nm
D_max	10.5	nm

SASDFK7 – ...histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O

Sample:	...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 D22, Institut Laue-Langevin (ILL) on 2016 Nov 14

Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 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

R_g^Guinier	1.9	nm
D_max	5.5	nm

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

SASDFM3 – ...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

SASDFN3 – ...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

SASDFP3 – ...histone chaperone Asf1, acetyltransferase Rtt109 and histones H3 and H4, 70%-2H histone chaperone Vps75 (1H Asf1-H3:H4-Rtt109, 2H(70%) Vps75) acquired in 100% v/v D2O

SASDFQ3 – ...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

SASDFR3 – ...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

SASDFK7 – ...histone chaperone Asf1, histones H3 (35-135aa) and H4; 70%-2H histone acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) acquired in 100% v/v D2O