Small Angle Scattering Biological Data Bank SASBDB


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217 hits found for sans

SASDS22 – Sulfite reductase flavoprotein crosslinked octamer

Sulfite reductase [NADPH] flavoprotein alpha-component experimental SAS data

Sample:	Sulfite reductase [NADPH] flavoprotein alpha-component octamer, 530 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jun 24

Domain crossover in the reductase subunit of NADPH-dependent assimilatory sulfite reductase. J Struct Biol 215(4):108028 (2023)
Walia N, Murray DT, Garg Y, He H, Weiss KL, Nagy G, Elizabeth Stroupe M

R_g^Guinier	8.4	nm
D_max	23.0	nm
Volume^Porod	767	nm³

SASDS32 – Reconstituted sulfite reductase crosslinked dodecamer with partially deuterated hemoprotein in 86% D2O

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) experimental SAS data

Sample:	Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) octamer, 566 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2023 Apr 24

R_g^Guinier	7.5	nm
D_max	22.6	nm
Volume^Porod	823	nm³

SASDS42 – Reconstituted sulfite reductase crosslinked dodecamer with partially deuterated hemoprotein in 41% D2O

Sample:	Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) octamer, 566 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Aug 24

R_g^Guinier	11.1	nm
D_max	32.4	nm
Volume^Porod	138	nm³

SASDN52 – SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 1.7

Sample:	Cytochrome c' monomer, 14 kDa Achromobacter xylosoxidans protein
Buffer:	Phosphate Buffer pD 1.7, pH: 1.7
Experiment:	SANS data collected at KWS1, FRM2 on 2017 Aug 12

Open-Bundle Structure as the Unfolding Intermediate of Cytochrome c′ Revealed by Small Angle Neutron Scattering Biomolecules 12(1):95 (2022)
Yamaguchi T, Akao K, Koutsioubas A, Frielinghaus H, Kohzuma T

R_g^Guinier	2.3	nm
D_max	8.6	nm
Volume^Porod	13	nm³

SASDS52 – Sulfite reductase crosslinked dodecamer

Sample:	Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) octamer, 566 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jul 15

R_g^Guinier	10.3	nm
D_max	31.0	nm
Volume^Porod	1170	nm³

SASDN62 – SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 6.4

Sample:	Cytochrome c' dimer, 27 kDa Alcaligenes protein
Buffer:	Phosphate Buffer pD 6.4, pH: 6.4
Experiment:	SANS data collected at KWS1, FRM2 on 2017 Aug 12

R_g^Guinier	1.8	nm
D_max	5.5	nm
Volume^Porod	11	nm³

SASDS62 – Sulfite reductase flavoprotein truncated linker (ΔAAPSQS) octamer

Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) experimental SAS data

Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) Kratky plot

Sample:	Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) octamer, 526 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jun 25

R_g^Guinier	13.7	nm
D_max	25.5	nm
Volume^Porod	961	nm³

SASDN72 – SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 9.6

Sample:	Cytochrome c' dimer, 27 kDa Alcaligenes protein
Buffer:	Phosphate Buffer pD 9.6, pH: 9.6
Experiment:	SANS data collected at KWS1, FRM2 on 2017 Aug 12

R_g^Guinier	1.9	nm
D_max	5.3	nm
Volume^Porod	10	nm³

SASDS72 – Sulfite reductase truncated linker (ΔAAPSQS) dodecamer

Sulfite reductase [NADPH] hemoprotein beta-componentSulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) experimental SAS data

Sulfite reductase [NADPH] hemoprotein beta-component Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) Kratky plot

Sample:	Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) octamer, 528 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jun 26

R_g^Guinier	10.8	nm
D_max	30.3	nm
Volume^Porod	1260	nm³

SASDN82 – SANS data from cytochrome c' from Alcaligenes xylosoxidans at pD = 13

Sample:	Cytochrome c' monomer, 14 kDa Achromobacter xylosoxidans protein
Buffer:	Phosphate Buffer pD 13, pH: 13
Experiment:	SANS data collected at KWS1, FRM2 on 2017 Aug 12

R_g^Guinier	4.8	nm
D_max	9.0	nm
Volume^Porod	20	nm³

SASDS82 – Reconstituted sulfite reductase crosslinked dodecamer with partially deuterated hemoprotein in 0% D2O

Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C)Sulfite reductase [NADPH] hemoprotein beta-component experimental SAS data

Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) Sulfite reductase [NADPH] hemoprotein beta-component Kratky plot

Sample:	Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) octamer, 566 kDa Escherichia coli (strain … protein Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jul 2

R_g^Guinier	9.5	nm
D_max	28.3	nm
Volume^Porod	1010	nm³

SASDS92 – Reconstituted sulfite reductase crosslinked dodecamer with partially deuterated hemoprotein in 100% D2O

Sulfite reductase [NADPH] hemoprotein beta-component Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) Kratky plot

Sample:	Sulfite reductase [NADPH] hemoprotein beta-component tetramer, 256 kDa Escherichia coli (strain … protein Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) octamer, 566 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jun 27

R_g^Guinier	8.2	nm
D_max	25.1	nm
Volume^Porod	839	nm³

SASDSA2 – Sulfite reductase flavoprotein reduced with 10 molar equivalents sodium dithionite

Sulfite reductase [NADPH] flavoprotein alpha-component Kratky plot

Sample:	Sulfite reductase [NADPH] flavoprotein alpha-component octamer, 530 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jul 15

R_g^Guinier	7.9	nm
D_max	27.6	nm
Volume^Porod	1060	nm³

SASDSB2 – Sulfite reductase flavoprotein crosslinked reduced with 10 molar equivalents sodium dithionite

Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) experimental SAS data

Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) Kratky plot

Sample:	Sulfite reductase [NADPH] flavoprotein alpha-component (E121C, C162T, C552S, N556C) octamer, 566 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jul 15

R_g^Guinier	8.0	nm
D_max	25.3	nm
Volume^Porod	827	nm³

SASDSC2 – Sulfite reductase truncated linker (ΔAAPSQS) flavoprotein reduced with 10 molar equivalents sodium dithionite

Sample:	Sulfite reductase [NADPH] flavoprotein alpha-component (Δ212-217) octamer, 526 kDa Escherichia coli (strain … protein
Buffer:	50 mM potassium phosphate, 100 mM NaCl, 1 mM EDTA, pH: 7.8
Experiment:	SANS data collected at ...SANS, Spallation Neutron Source on 2022 Jul 15

R_g^Guinier	7.6	nm
D_max	25.0	nm
Volume^Porod	952	nm³

SASDNK2 – ...SANS in 100% D2O

75% deuterated Circadian clock protein KaiBCircadian clock protein KaiA75% deuterated Circadian clock protein kinase KaiC (S431D mutant) experimental SAS data

Sample:	75% deuterated Circadian clock protein KaiB hexamer, 71 kDa Synechococcus elongatus (strain … protein Circadian clock protein KaiA dodecamer, 393 kDa Synechococcus elongatus (strain … protein 75% deuterated Circadian clock protein kinase KaiC (S431D mutant) hexamer, 357 kDa Synechococcus elongatus (strain … protein
Buffer:	50 mM sodium phosphate buffer, 150 mm NaCl, 5 mM MgCl2, 0.5 mM EDTA, 1 mM ATP, 1 mM DTT, 50 mM arginine, 50 mM glutamine, in 100% D2O, pH: 7.8
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Sep 19

Overall structure of fully assembled cyanobacterial KaiABC circadian clock complex by an integrated experimental-computational approach. Commun Biol 5(1):184 (2022)
Yunoki Y, Matsumoto A, Morishima K, Martel A, Porcar L, Sato N, Yogo R, Tominaga T, Inoue R, Yagi-Utsumi M, Okuda A, Shimizu M, Urade R, Terauchi K, Kono H, Yagi H, Kato K, Sugiyama M

R_g^Guinier	7.8	nm
D_max	25.6	nm
Volume^Porod	1620	nm³

SASDMU2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) without Dox monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

...SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI

R_g^Guinier	6.1	nm
D_max	20.5	nm

SASDGV2 – ...SANS data in 42% v/v D2O)

Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase50S ribosomal protein L7AeNOP5/NOP56 related proteinpyrococcus furiosus sR26 stabilized constructPyrococcus furiosus sR26 substrate D' experimental SAS data

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at KWS1, FRM2 on 2015 May 24

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.9	nm
D_max	16.0	nm
Volume^Porod	87	nm³

SASDMV2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - 5α-cholestan-3-one) with Dox (10%) monomer, 220 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	7.5	nm
D_max	25.5	nm

SASDGW2 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Sep 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.1	nm
D_max	14.0	nm
Volume^Porod	210	nm³

SASDMW2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) without Dox monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	6.4	nm
D_max	22.5	nm

SASDGX2 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Nov 23

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.0	nm
D_max	13.3	nm
Volume^Porod	42	nm³

SASDMX2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Opb-Chol) with Dox (10%) monomer, 225 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	10.0	nm
D_max	21.9	nm

SASDGY2 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jul 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	2.8	nm
D_max	9.9	nm
Volume^Porod	52	nm³

SASDMY2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	6.5	nm
D_max	22.9	nm

SASDGZ2 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at KWS1, FRM2 on 2015 May 23

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.8	nm
D_max	16.6	nm
Volume^Porod	82	nm³

SASDMZ2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	6.9	nm
D_max	23.8	nm

SASDG23 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D' monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Apr 8

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.0	nm
D_max	13.8	nm
Volume^Porod	214	nm³

SASDM23 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 16

R_g^Guinier	5.9	nm
D_max	19.7	nm

SASDG33 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Apr 8

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.0	nm
D_max	13.9	nm
Volume^Porod	231	nm³

SASDL33 – ...SANS

Proton-gated ion channel experimental SAS data

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Aug 22

Probing solution structure of the pentameric ligand-gated ion channel GLIC by small-angle neutron scattering Proceedings of the National Academy of Sciences 118(37):e2108006118 (2021)
Lycksell M, Rovšnik U, Bergh C, Johansen N, Martel A, Porcar L, Arleth L, Howard R, Lindahl E

R_g^Guinier	3.8	nm
D_max	13.5	nm
Volume^Porod	274	nm³

SASDM33 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	5.5	nm
D_max	18.3	nm

SASDG43 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at KWS1, FRM2 on 2015 May 24

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.9	nm
D_max	16.6	nm
Volume^Porod	65	nm³

SASDL43 – ...SANS

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM citrate, 150 mM NaCl, 0.5 mM match-out deuterated DDM, pH: 3
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Aug 22

R_g^Guinier	3.8	nm
D_max	12.7	nm
Volume^Porod	279	nm³

SASDG53 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Sep 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	4.1	nm
D_max	14.0	nm
Volume^Porod	222	nm³

SASDL53 – ...SANS

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jun 20

R_g^Guinier	3.8	nm
D_max	12.0	nm
Volume^Porod	235	nm³

SASDG63 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2015 Nov 23

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	3.9	nm
D_max	12.5	nm
Volume^Porod	49	nm³

SASDJ63 – Streptococcus pneumoniae NADPH oxidase - Tag-free SpNOX

FAD-binding FR-type domain-containing protein experimental SAS data

Sample:	FAD-binding FR-type domain-containing protein monomer, 47 kDa Streptococcus pneumoniae protein
Buffer:	50 mM Tris-HCl pH 7, 300 mM NaCl, 5 mM LMNG, 10 µM FAD, 21.4% D₂O, pH: 7
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2018 Jun 26

...SANS Using LMNG Stealth Carrier. Biophys J 119(3):605-618 (2020)
Vermot A, Petit-Härtlein I, Breyton C, Le Roy A, Thépaut M, Vivès C, Moulin M, Härtlein M, Grudinin S, Smith SME, Ebel C, Martel A, Fieschi F

R_g^Guinier	3.0	nm
D_max	10.0	nm
Volume^Porod	89	nm³

SASDL63 – ...SANS

Sample:	Proton-gated ion channel pentamer, 183 kDa Gloeobacter violaceus (strain … protein
Buffer:	D2O, 20 mM Tris, 150 mM NaCl, 0.5 mM matched-out deuterated DDM,, pH: 7.5
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jun 21

R_g^Guinier	4.0	nm
D_max	17.7	nm
Volume^Porod	225	nm³

SASDG73 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2019 Jul 21

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	2.7	nm
D_max	9.5	nm
Volume^Porod	25	nm³

SASDG83 – ...SANS data in 42% v/v D2O)

Sample:	Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase dimer, 52 kDa Pyrococcus furiosus protein 50S ribosomal protein L7Ae dimer, 27 kDa Pyrococcus furiosus protein NOP5/NOP56 related protein dimer, 94 kDa Pyrococcus furiosus protein pyrococcus furiosus sR26 stabilized construct monomer, 24 kDa Pyrococcus furiosus RNA Pyrococcus furiosus sR26 substrate D monomer, 4 kDa Pyrococcus furiosus RNA
Buffer:	50 mM phosphate 500 mM NaCl 42%D2O, pH: 6.6
Experiment:	SANS data collected at KWS1, FRM2 on 2015 May 23

The guide sRNA sequence determines the activity level of box C/D RNPs. Elife 9 (2020)
Graziadei A, Gabel F, Kirkpatrick J, Carlomagno T

R_g^Guinier	5.1	nm
D_max	15.5	nm
Volume^Porod	125	nm³

SASDRE3 – Tissue Transglutaminase + Ca: Time-resolved 0ms

Protein-glutamine gamma-glutamyltransferase 2 experimental SAS data

Protein-glutamine gamma-glutamyltransferase 2 Kratky plot

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

Chaotic advection mixer for capturing transient states of diverse biological macromolecular systems with time-resolved small-angle X-ray scattering IUCrJ 10(3):363-375 (2023)
Zielinski K, Katz A, Calvey G, Pabit S, Milano S, Aplin C, San Emeterio J, Cerione R, Pollack L

R_g^Guinier	4.1	nm
D_max	16.0	nm
Volume^Porod	150	nm³

SASDRF3 – Tissue Transglutaminase + Ca: Time-resolved 32 ms

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	4.1	nm
D_max	17.0	nm
Volume^Porod	170	nm³

SASDRG3 – Tissue Transglutaminase + Ca: Time-resolved 63 ms

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	4.1	nm
D_max	18.0	nm
Volume^Porod	155	nm³

SASDRH3 – Tissue Transglutaminase + Ca: Time-resolved 100 ms

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	4.1	nm
D_max	20.0	nm
Volume^Porod	190	nm³

SASDRJ3 – Tissue Transglutaminase + Ca: Time-resolved 316 ms

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	4.5	nm
D_max	24.0	nm
Volume^Porod	200	nm³

SASDRK3 – Tissue Transglutaminase + Ca: Time-resolved 631 ms

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	4.6	nm
D_max	26.0	nm
Volume^Porod	215	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

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

SASDRL3 – Tissue Transglutaminase + Ca: Time-resolved 1500 ms

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	4.6	nm
D_max	28.0	nm
Volume^Porod	230	nm³

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

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

SASDRM3 – Tissue Transglutaminase + Ca: 5min Equilibrium

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Sep 29

R_g^Guinier	5.0	nm
D_max	27.0	nm
Volume^Porod	241	nm³

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

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

SASDRN3 – Tissue Transglutaminase + Ca: 10min Equilibrium

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Nov 19

R_g^Guinier	5.5	nm
D_max	26.0	nm
Volume^Porod	300	nm³

SASDRP3 – Tissue Transglutaminase + Ca: 30min Equilibrium

Sample:	Protein-glutamine gamma-glutamyltransferase 2 , 77 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 100 mM NaCl, 10% glycerol, 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at ID7A1 BioSAXS / HP-Bio Beamline, Cornell High Energy Synchrotron Source (CHESS) on 2021 Sep 29

R_g^Guinier	6.9	nm
D_max	31.5	nm
Volume^Porod	490	nm³

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

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

SASDRQ3 – Trypsin + Aprotinin: Time-Resolved 10 ms

Serine protease 1Pancreatic trypsin inhibitor experimental SAS data

Serine protease 1 Pancreatic trypsin inhibitor Kratky plot

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.9	nm
D_max	5.3	nm
Volume^Porod	23	nm³

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

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

SASDRR3 – Trypsin + Aprotinin: Time-Resolved 30 ms

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.9	nm
D_max	5.3	nm
Volume^Porod	28	nm³

SASDRS3 – Trypsin + Aprotinin: Time-Resolved 100 ms

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.8	nm
D_max	5.3	nm
Volume^Porod	30	nm³

SASDRT3 – Trypsin + Aprotinin: Time-Resolved 400 ms

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.9	nm
D_max	5.3	nm
Volume^Porod	27	nm³

SASDRU3 – Trypsin + Aprotinin: Time-Resolved 630 ms

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.9	nm
D_max	5.3	nm
Volume^Porod	25	nm³

SASDRV3 – Trypsin + Aprotinin: Time-Resolved 1000 ms

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.8	nm
D_max	5.3	nm
Volume^Porod	28	nm³

SASDRW3 – Trypsin + Aprotinin: Time-Resolved 2000 ms

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.0	nm
D_max	5.3	nm
Volume^Porod	29	nm³

SASDRX3 – Trypsin + Aprotinin: Complex equilibrium

Sample:	Serine protease 1 monomer, 26 kDa Bos taurus protein Pancreatic trypsin inhibitor monomer, 11 kDa Bos taurus protein
Buffer:	20 mM TRIS, 40 mM KCl, 20 mM CaCl2, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	1.9	nm
D_max	5.3	nm
Volume^Porod	31	nm³

SASDRY3 – Kenics GAC rRNA + Mg: Time-Resolved 10 ms

58 nucleotide RNA L11-binding domain from E. coli 23S rRNA experimental SAS data

58 nucleotide RNA L11-binding domain from E. coli 23S rRNA Kratky plot

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.2	nm
D_max	10.0	nm
Volume^Porod	28	nm³

SASDRZ3 – Kenics GAC rRNA + Mg: Time-Resolved 32 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.2	nm
D_max	10.0	nm
Volume^Porod	27	nm³

SASDR24 – Kenics GAC rRNA + Mg: Time-Resolved 63 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.2	nm
D_max	9.5	nm
Volume^Porod	27	nm³

SASDP34 – ...SANS data at 0% v/v D2O, plus additional SANS with contrast variation and SAXS datasets)

Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S)Ubiquitin experimental SAS data

Sample:	Ubiquitin-conjugating enzyme E2 D1 (S22R, C85K, D87S) monomer, 17 kDa Homo sapiens protein Ubiquitin monomer, 9 kDa Homo sapiens protein
Buffer:	50 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment:	SANS data collected at Quokka - Small Angle Neutron Scattering, Australian Centre for Neutron Scattering (ANSTO) on 2019 May 24

Production and characterisation of modularly deuterated UBE2D1–Ub conjugate by small angle neutron and X-ray scattering European Biophysics Journal (2022)
Pietras Z, Duff A, Morad V, Wood K, Jeffries C, Sunnerhagen M

R_g^Guinier	2.1	nm
D_max	7.4	nm

SASDR34 – Kenics GAC rRNA + Mg: Time-Resolved 100 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.2	nm
D_max	10.0	nm
Volume^Porod	28	nm³

SASDR44 – Kenics GAC rRNA + Mg: Time-Resolved 316 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.2	nm
D_max	12.0	nm
Volume^Porod	27	nm³

SASDR54 – Kenics GAC rRNA + Mg: Time-Resolved 631 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.3	nm
D_max	9.8	nm
Volume^Porod	26	nm³

SASDR64 – Kenics GAC rRNA + Mg: Time-Resolved 1000 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.3	nm
D_max	11.0	nm
Volume^Porod	26	nm³

SASDR74 – Kenics GAC rRNA + Mg: Equilibrium initial

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.4	nm
D_max	10.0	nm
Volume^Porod	32	nm³

SASDR84 – Kenics GAC rRNA + Mg: Equilibrium final

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.2	nm
D_max	10.0	nm
Volume^Porod	26	nm³

SASDR94 – GAC rRNA + L11 Protein: Time-Resolved 30 ms

58 nucleotide RNA L11-binding domain from E. coli 23S rRNA50S ribosomal protein L11 experimental SAS data

58 nucleotide RNA L11-binding domain from E. coli 23S rRNA 50S ribosomal protein L11 Kratky plot

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.4	nm
D_max	12.0	nm
Volume^Porod	34	nm³

SASDRA4 – GAC rRNA + L11 Protein: Time-Resolved 50 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.5	nm
D_max	13.5	nm
Volume^Porod	36	nm³

SASDRB4 – GAC rRNA + L11 Protein: Time-Resolved 63 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.4	nm
D_max	11.5	nm
Volume^Porod	33	nm³

SASDRC4 – GAC rRNA + L11 Protein: Time-Resolved 100 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.4	nm
D_max	11.5	nm
Volume^Porod	35	nm³

SASDJD4 – Bacteriorhodopsin solubilized in contrast-matched octyl glucoside

Sample:	Bacteriorhodopsin monomer, 27 kDa Halobacterium salinarum protein
Buffer:	25 mM NaH2PO4, 1.35 mM KOH, 40 mM partially-deuterated octyl glucoside mixture, pH: 5.6
Experiment:	SANS data collected at ...SANS, NIST Center for High Resolution Neutron Scattering (CHRNS) on 2017 Jan 20

Direct localization of detergents and bacteriorhodopsin in the lipidic cubic phase by small-angle neutron scattering IUCrJ 8(1) (2021)
Cleveland IV T, Blick E, Krueger S, Leung A, Darwish T, Butler P

R_g^Guinier	2.7	nm
D_max	5.4	nm
Volume^Porod	68	nm³

SASDRD4 – GAC rRNA + L11 Protein: Time-Resolved 200 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.5	nm
D_max	12.5	nm
Volume^Porod	37	nm³

SASDRE4 – GAC rRNA + L11 Protein: Time-Resolved 316 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.5	nm
D_max	10.0	nm
Volume^Porod	38	nm³

SASDRF4 – GAC rRNA + L11 Protein: Time-Resolved 631 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.5	nm
D_max	13.0	nm
Volume^Porod	38	nm³

SASDRG4 – GAC rRNA + L11 Protein: Time-Resolved 1000 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.5	nm
D_max	12.5	nm
Volume^Porod	40	nm³

SASDRH4 – GAC rRNA + L11 Protein: Time-Resolved 2000 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2018 May 9

R_g^Guinier	2.6	nm
D_max	12.8	nm
Volume^Porod	39	nm³

SASDRJ4 – GAC rRNA + L11 Protein: SEC-SAXS final

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA 50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM Na-MOPSO, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Nov 19

R_g^Guinier	2.6	nm
D_max	13.0	nm
Volume^Porod	48	nm³

SASDRK4 – Diffusive GAC rRNA + Mg: Time-Resolved 10 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.2	nm
D_max	12.0	nm
Volume^Porod	29	nm³

SASDRL4 – Diffusive GAC rRNA + Mg: Time-Resolved 30 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.2	nm
D_max	12.0	nm
Volume^Porod	29	nm³

SASDRM4 – Diffusive GAC rRNA + Mg: Time-Resolved 100 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.2	nm
D_max	9.0	nm
Volume^Porod	29	nm³

SASDRN4 – Diffusive GAC rRNA + Mg: Time-Resolved 300 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.2	nm
D_max	12.0	nm
Volume^Porod	29	nm³

SASDRP4 – Diffusive GAC rRNA + Mg: Time-Resolved 1000 ms

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.4	nm
D_max	13.0	nm
Volume^Porod	30	nm³

SASDRQ4 – Diffusive GAC rRNA + Mg: Equilibrium initial

Sample:	58 nucleotide RNA L11-binding domain from E. coli 23S rRNA monomer, 19 kDa Escherichia coli RNA
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.4	nm
D_max	10.0	nm
Volume^Porod	34	nm³

SASDRR4 – Diffusive GAC rRNA + Mg: Equilibrium final

50S ribosomal protein L11 experimental SAS data

Sample:	50S ribosomal protein L11 monomer, 16 kDa Thermus thermophilus protein
Buffer:	10 mM sodium cacodylate, 100 mM KCl, pH: 6.5
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 9

R_g^Guinier	2.2	nm
D_max	11.0	nm
Volume^Porod	27	nm³

SASDES4 – ...SANS, 100% D2O)

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data

Sample:	Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer:	30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment:	SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28

Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H

R_g^Guinier	4.0	nm
D_max	13.0	nm
Volume^Porod	202	nm³

SASDDT4 – Fc region of Immunoglobulin G1 (IgG1 Fc)

Immunoglobulin heavy constant gamma 1 experimental SAS data

Sample:	Immunoglobulin heavy constant gamma 1 dimer, 53 kDa Homo sapiens protein
Buffer:	20mM HEPES, 50mM NaCl, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17

Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M

R_g^Guinier	2.6	nm
D_max	10.0	nm
Volume^Porod	70	nm³

SASDET4 – ...SANS, 100% D2O)

ACA8 complex with Calmodulin (75% deuterated) in stealth nanodisc (SANS, 100% D2O) Rg histogram

Sample:	Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein Calmodulin-7 (deuterated 75%) monomer, Arabidopsis thaliana protein
Buffer:	30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment:	SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28

R_g^Guinier	4.3	nm
D_max	15.0	nm
Volume^Porod	217	nm³

SASDDU4 – Fc region of Immunoglobulin G2 (IgG2 Fc)

Immunoglobulin heavy constant gamma 2 experimental SAS data

Sample:	Immunoglobulin heavy constant gamma 2 dimer, 52 kDa Homo sapiens protein
Buffer:	20mM HEPES, 50mM NaCl, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17

Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M

R_g^Guinier	2.8	nm
D_max	9.0	nm
Volume^Porod	67	nm³

SASDEU4 – ...SANS, 100% D2O)

Sample:	Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein Calmodulin-7 monomer, Arabidopsis thaliana protein
Buffer:	30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment:	SANS data collected at SANS-1, Heinz Maier-Leibnitz Zentrum on 2017 Aug 28

R_g^Guinier	4.8	nm
D_max	18.0	nm
Volume^Porod	297	nm³

SASDPU4 – ...SANS Profile - Ribonuclease A in 100% v/v D2O buffer

Ribonuclease pancreatic experimental SAS data

Sample:	Ribonuclease pancreatic monomer, 14 kDa Bos taurus protein
Buffer:	50 mM Tris, 100 mM NaCl, pH: 7.5
Experiment:	SANS data collected at (Consensus SAS), Multi-facility, Multiple countries on 2022 Jun 6

A round-robin approach provides a detailed assessment of biomolecular small-angle scattering data reproducibility and yields consensus curves for benchmarking Acta Crystallographica Section D Structural Biology 78(11) (2022)
Trewhella J, Vachette P, Bierma J, Blanchet C, Brookes E, Chakravarthy S, Chatzimagas L, Cleveland T, Cowieson N, Crossett B, Duff A, Franke D, Gabel F, Gillilan R, Graewert M, Grishaev A, Guss J, Ham...

R_g^Guinier	1.4	nm
D_max	4.4	nm

SASDDV4 – Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE)

Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E experimental SAS data

Sample:	Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E dimer, 53 kDa Homo sapiens protein
Buffer:	20 mM HEPES, 50mM NaCl, pH: 7.5
Experiment:	SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17

Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M

R_g^Guinier	2.7	nm
D_max	10.0	nm
Volume^Porod	74	nm³

SASDPV4 – ...SANS Profile - Lysozyme in 100% v/v D2O buffer

Sample:	Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer:	50 mM sodium citrate, 150 mM NaCl, pH: 4.5
Experiment:	SANS data collected at (Consensus SAS), Multi-facility, Multiple countries on 2022 Jun 6

R_g^Guinier	1.2	nm
D_max	3.8	nm

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