Small Angle Scattering Biological Data Bank SASBDB


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23 hits found for Histone H4

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:	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

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:	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

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:	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

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:	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 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:	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, 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:	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, 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

SASDFX3 – Semi-synthetic nucleosome core particle (NCP)

Histone H3Histone H4Histone H2aHistone H2b147bp 601 Widom sequence experimental SAS data

Histone H3 Histone H4 Histone H2a Histone H2b 147bp 601 Widom sequence Kratky plot

Sample:	Histone H3 dimer, 31 kDa Xenopus laevis protein Histone H4 dimer, 22 kDa Xenopus laevis protein Histone H2a dimer, 28 kDa Xenopus laevis protein Histone H2b dimer, 27 kDa Xenopus laevis protein 147bp 601 Widom sequence monomer, 45 kDa synthetic construct DNA
Buffer:	15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment:	SAXS data collected at BM29, ESRF on 2017 Dec 11

A Tail-Based Mechanism Drives Nucleosome Demethylation by the LSD2/NPAC Multimeric Complex. Cell Rep 27(2):387-399.e7 (2019)
Marabelli C, Marrocco B, Pilotto S, Chittori S, Picaud S, Marchese S, Ciossani G, Forneris F, Filippakopoulos P, Schoehn G, Rhodes D, Subramaniam S, Mattevi A

R_g^Guinier	4.4	nm
D_max	12.8	nm
Volume^Porod	353	nm³

SASDFY3 – Semi-synthetic nucleosome core particle (NCP) in complex with lysine-specific demethylase (LSD2) and the dehydrogenase domain plus linker of cytokine-like nuclear factor (NPAC delta-205)

Lysyne-specific Demethylase LSD2NPAC linker+DH (delta-205)Histone H3Histone H4Histone H2aHistone H2b147bp 601 Widom sequence experimental SAS data

Lysyne-specific Demethylase LSD2 NPAC linker+DH (delta-205) Histone H3 Histone H4 Histone H2a Histone H2b 147bp 601 Widom sequence Kratky plot

Sample:	Lysyne-specific Demethylase LSD2 monomer, 89 kDa Homo sapiens protein NPAC linker+DH (delta-205) tetramer, 150 kDa Homo sapiens protein Histone H3 dimer, 31 kDa Xenopus laevis protein Histone H4 dimer, 22 kDa Xenopus laevis protein Histone H2a dimer, 28 kDa Xenopus laevis protein Histone H2b dimer, 27 kDa Xenopus laevis protein 147bp 601 Widom sequence monomer, 45 kDa synthetic construct DNA
Buffer:	15 mM HEPES, 200 mM NaCl, pH: 7.3
Experiment:	SAXS data collected at BM29, ESRF on 2017 Dec 11

R_g^Guinier	7.8	nm
D_max	30.4	nm
Volume^Porod	1100	nm³

SASDJJ5 – Histone H2A:H2B:H3:H4 complex with aprataxin and polynucleotide kinase like factor (APLF) acidic domain

Aprataxin and PNK-like factor (acidic domain)Histone H2AHistone H2BHistone H3Histone H4 experimental SAS data

Sample:	Aprataxin and PNK-like factor (acidic domain) dimer, 15 kDa Homo sapiens protein Histone H2A dimer, 26 kDa Drosophila melanogaster protein Histone H2B dimer, 27 kDa Drosophila melanogaster protein Histone H3 dimer, 30 kDa Drosophila melanogaster protein Histone H4 dimer, 23 kDa Drosophila melanogaster protein
Buffer:	25 mM NaPi, 300 mM NaCl, 3% v/v glycerol, 1 mM DTT,, pH: 7
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2018 Jul 10

...histone octamer by the acidic domain of DNA repair factor APLF. Sci Adv 8(30):eabo0517 (2022)
Corbeski I, Guo X, Eckhardt BV, Fasci D, Wiegant W, Graewert MA, Vreeken K, Wienk H, Svergun DI, Heck AJR, van Attikum H, Boelens R, Sixma TK, Mattiroli F, van Ingen H

R_g^Guinier	3.7	nm
D_max	10.8	nm
Volume^Porod	260	nm³

SASDJ96 – Trinucleosomes from Xenopus laevis (African clawed frog)

Histone H3Histone H4Histone H2A type 1Histone H2BNon-linker Ended Trinucleosome DNA experimental SAS data

Histone H3 Histone H4 Histone H2A type 1 Histone H2B Non-linker Ended Trinucleosome DNA Kratky plot

Sample:	Histone H3 monomer, 15 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein Histone H2B monomer, 14 kDa Xenopus laevis protein Non-linker Ended Trinucleosome DNA monomer, 172 kDa DNA
Buffer:	20 mM Tris 150 mM NaCl 1 mM EDTA 1 mM DTT 50% w/v sucrose, pH: 7.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Mar 11

Solution structure(s) of trinucleosomes from contrast variation SAXS Nucleic Acids Research (2021)
Mauney A, Muthurajan U, Luger K, Pollack L

R_g^Guinier	12.9	nm
D_max	41.8	nm

SASDCT6 – 12N12 nucleosome in 60% sucrose with ADP-BeF3

169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data

12N12 nucleosome in 60% sucrose with ADP-BeF3 Rg histogram

Sample:	169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein Histone H3.2 monomer, 15 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer:	10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH: 7.8
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24

The ATPase motor of the Chd1 chromatin remodeler stimulates DNA unwrapping from the nucleosome. Nucleic Acids Res 46(10):4978-4990 (2018)
Tokuda JM, Ren R, Levendosky RF, Tay RJ, Yan M, Pollack L, Bowman GD

R_g^Guinier	4.8	nm
D_max	14.0	nm

SASDCU6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose without any nucleotides added (Apo)

Chromodomain-helicase-DNA-binding protein 1169 bp DNA (145 bp Widom 601, flanked by 12bp DNA)Histone H2A type 1Histone H2B 1.1Histone H3.2Histone H4 experimental SAS data

Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose without any nucleotides added (Apo) Rg histogram

Sample:	Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein Histone H3.2 monomer, 15 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer:	10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, pH: 7.8
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24

R_g^Guinier	5.2	nm
D_max	12.8	nm

SASDCV6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3

Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with ADP-BeF3 Rg histogram

Sample:	Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein Histone H3.2 monomer, 15 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer:	10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, ADP-BeF3 (0.5 mM ADP, 4 mM NaF, 0.6 mM BeCl2), pH: 7.8
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24

R_g^Guinier	5.3	nm
D_max	16.5	nm

SASDCW6 – Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with AMP-PNP

Chd1-12N12, chromatin remodeler--nucleosome complex, in 60% sucrose with AMP-PNP Rg histogram

Sample:	Chromodomain-helicase-DNA-binding protein 1 dimer, 266 kDa Saccharomyces cerevisiae protein 169 bp DNA (145 bp Widom 601, flanked by 12bp DNA) monomer, 52 kDa DNA Histone H2A type 1 monomer, 14 kDa Xenopus laevis protein Histone H2B 1.1 monomer, 14 kDa Xenopus laevis protein Histone H3.2 monomer, 15 kDa Xenopus laevis protein Histone H4 monomer, 11 kDa Xenopus laevis protein
Buffer:	10 mM Tris, 100 mM NaCl, 2 mM MgCl2, 0.1 mM EDTA, 1 mM DTT, 60% (w/v) sucrose, 0.5 mM AMP-PNP, pH: 7.8
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 24

R_g^Guinier	5.6	nm
D_max	16.7	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:	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 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

SASDFL7 – ...histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data

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

R_g^Guinier	3.4	nm
D_max	10.5	nm

SASDFM7 – ...histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (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

R_g^Guinier	2.7	nm
D_max	9.0	nm

SASDFN7 – ...histone acetyltransferase Rtt109 with histones H3 and H4, histone chaperones Asf1 and 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 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

R_g^Guinier	3.5	nm
D_max	11.0	nm

SASDFP7 – ...histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O

Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-lengthVacuolar protein sorting-associated protein 75 full-length experimental SAS data

Sample:	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 Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae 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 Jun 9

R_g^Guinier	3.5	nm
D_max	11.5	nm

SASDFQ7 – ...histone chaperone Vps75, histones H3 and H4, 2H histone chaperone Asf1, histone acetyltransferase Rtt109, acquired in 42% v/v D2O

Sample:	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 Vacuolar protein sorting-associated protein 75 full-length dimer, 61 kDa Saccharomyces cerevisiae 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 Jun 9

R_g^Guinier	3.1	nm
D_max	9.5	nm

SASDBS7 – Nucleosome Core Particle: 1.2 M NaCl, 50% sucrose, 50ms - 10s time resolved data

Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B HeterodimerNucleasome Core Particle with Widom 601 DNA - HISTONE H3-H4 HeterodimerNucleasome Core Particle with Widom 601 DNA - dsDNA experimental SAS data

Sample:	...HISTONE H2A-H2B Heterodimer dimer, 48 kDa Xenopus laevis protein ...HISTONE H3-H4 Heterodimer dimer, 46 kDa Xenopus laevis protein Nucleasome Core Particle with Widom 601 DNA - dsDNA monomer, 92 kDa Xenopus laevis DNA
Buffer:	20 mM Tris-Cl, 0.1 mM EDTA, 0.1 mM DTT, 50% sucrose, 1.2 M NaCl, pH: 7.5
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Apr 14

...histone core. Proc Natl Acad Sci U S A 114(2):334-339 (2017)
Chen Y, Tokuda JM, Topping T, Meisburger SP, Pabit SA, Gloss LM, Pollack L

R_g^Guinier

5.8

SASDBT7 – Nucleosome Core Particle: 1.9 M NaCl, 50% sucrose, 50ms - 10s time resolved data

Sample:	...HISTONE H2A-H2B Heterodimer dimer, 48 kDa Xenopus laevis protein ...HISTONE H3-H4 Heterodimer dimer, 46 kDa Xenopus laevis protein Nucleasome Core Particle with Widom 601 DNA - dsDNA monomer, 92 kDa Xenopus laevis DNA
Buffer:	20 mM Tris-Cl, 0.1 mM EDTA, 0.1 mM DTT, 50% sucrose, 1.9 M NaCl, pH: 7.5
Experiment:	SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Apr 14

...histone core. Proc Natl Acad Sci U S A 114(2):334-339 (2017)
Chen Y, Tokuda JM, Topping T, Meisburger SP, Pabit SA, Gloss LM, Pollack L

R_g^Guinier

6.8

SASDNS7 – ...H4 histone oligomer complex

Peptidyl-prolyl cis-trans isomerase FKBP43Histone H3.1Histone H4 experimental SAS data

Sample:	Peptidyl-prolyl cis-trans isomerase FKBP43 pentamer, 81 kDa Arabidopsis thaliana protein Histone H3.1 dimer, 31 kDa Homo sapiens protein Histone H4 dimer, 23 kDa Homo sapiens protein
Buffer:	20 mM Tris, 300 mM NaCl, 1 mM β-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at BM29, ESRF on 2021 Apr 28

...histone interaction. Biochim Biophys Acta Gene Regul Mech 1865(7):194872 (2022)
Singh AK, Saharan K, Baral S, Vasudevan D

R_g^Guinier	4.4	nm
D_max	14.1	nm
Volume^Porod	226	nm³

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