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97 hits found for Chen

SASDF22 – Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the human growth hormone derivative somapacitan.

somapacitanFcRn binding optimised human serum albumin  V418M, T420A, E505G, V547Aneonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tagneonatal Fc receptor ectodomain alpha-chain experimental SAS data
somapacitan FcRn binding optimised human serum albumin  V418M, T420A, E505G, V547A neonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tag neonatal Fc receptor ectodomain alpha-chain Kratky plot
Sample: somapacitan monomer, 22 kDa Homo sapiens protein
FcRn binding optimised human serum albumin V418M, T420A, E505G, V547A monomer, 66 kDa Homo sapiens protein
neonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tag monomer, 13 kDa Homo sapiens protein
neonatal Fc receptor ectodomain alpha-chain monomer, 30 kDa Homo sapiens protein
Buffer: 100 mM MES, 100 mM NaCl, pH: 6.5
Experiment: SAXS data collected at I911-4, MAX IV on 2015 May 11
Identification of binding sites on human serum albumin for somapacitan - a long-acting growth hormone derivative. Biochemistry (2020)
...Chen J, Jensen S, Petersen J, Thygesen P
RgGuinier 4.2 nm
Dmax 14.7 nm
VolumePorod 227 nm3

SASDF32 – Ternary complex of FcRn ectodomain, FcRn binding optimised human serum albumin and the albumin-binding side chain of the human growth hormone derivative somapacitan.

FcRn binding optimised human serum albumin  V418M, T420A, E505G, V547Aneonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tagAlbumin-binding side-chainneonatal Fc receptor ectodomain alpha-chain experimental SAS data
FcRn binding optimised human serum albumin  V418M, T420A, E505G, V547A neonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tag Albumin-binding side-chain neonatal Fc receptor ectodomain alpha-chain Kratky plot
Sample: FcRn binding optimised human serum albumin V418M, T420A, E505G, V547A monomer, 66 kDa Homo sapiens protein
neonatal Fc receptor ectodomain beta-microglogulin part with C-terminal His6 tag monomer, 13 kDa Homo sapiens protein
Albumin-binding side-chain monomer, 1 kDa
neonatal Fc receptor ectodomain alpha-chain monomer, 30 kDa Homo sapiens protein
Buffer: 100 mM MES, 100 mM NaCl, pH: 6.5
Experiment: SAXS data collected at I911-4, MAX IV on 2015 Nov 11
Identification of binding sites on human serum albumin for somapacitan - a long-acting growth hormone derivative. Biochemistry (2020)
...Chen J, Jensen S, Petersen J, Thygesen P
RgGuinier 3.6 nm
Dmax 12.6 nm
VolumePorod 174 nm3

SASDF42 – Human serum albumin in complex with somapacitan

Human serum albuminSomapacitan experimental SAS data
SASREF model
Sample: Human serum albumin monomer, 66 kDa Homo sapiens protein
Somapacitan dimer, 44 kDa Homo sapiens protein
Buffer: 100 mM MES, 140 mM NaCl, pH: 6.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, Novo Nordisk A/S on 2015 Sep 4
Identification of binding sites on human serum albumin for somapacitan - a long-acting growth hormone derivative. Biochemistry (2020)
...Chen J, Jensen S, Petersen J, Thygesen P
RgGuinier 4.1 nm
Dmax 13.9 nm
VolumePorod 202 nm3

SASDF52 – dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

Dosage compensation regulator experimental SAS data
dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE Rg histogram
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
...Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 22 nm3

SASDF62 – Mixture of the dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE, and the roX2 RNA stem-loop 7 18mer-fragment, at 1.0 mg/ml

Dosage compensation regulatorroX2 stem-loop 7, 18-mer fragment experimental SAS data
Dosage compensation regulator roX2 stem-loop 7, 18-mer fragment Kratky plot
Sample: Dosage compensation regulator monomer, 29 kDa Drosophila melanogaster protein
roX2 stem-loop 7, 18-mer fragment monomer, 12 kDa synthetic construct RNA
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
...Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.1 nm
Dmax 13.3 nm
VolumePorod 25 nm3

SASDF72 – roX2 RNA stem-loop 7 18mer-fragment

roX2 stem-loop 7, 18-mer fragment experimental SAS data
DAMMIN model
Sample: roX2 stem-loop 7, 18-mer fragment monomer, 12 kDa synthetic construct RNA
Buffer: 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Nov 29
Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless. Nucleic Acids Res 47(8):4319-4333 (2019)
...Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 1.8 nm
Dmax 8.5 nm
VolumePorod 14 nm3

SASDK82 – Full-length nonstructural protein 2 (nsP2) of Chikungunya virus (CHIKV)

NsP2 protein experimental SAS data
CORAL model
Sample: NsP2 protein monomer, 90 kDa Chikungunya virus protein
Buffer: 20 mM Hepes pH 7.4, 150 mM NaCl, 1 mM DTT, 5% glycerol, pH: 7.4
Experiment: SAXS data collected at 23A, Taiwan Light Source on 2019 Aug 10
Inter-domain Flexibility of Chikungunya Virus nsP2 Helicase-Protease Differentially Influences Viral RNA Replication and Infectivity. J Virol (2020)
...Chen MW, Jeng US, Merits A, Luo D
RgGuinier 3.9 nm
Dmax 12.0 nm
VolumePorod 134 nm3

SASDED2 – Polyglutamine tract-binding protein 1 (PQBP-1)

Polyglutamine-binding protein 1 experimental SAS data
Polyglutamine tract-binding protein 1 (PQBP-1) Rg histogram
Sample: Polyglutamine-binding protein 1 monomer, 31 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1mM DTT,, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III on 2009 Nov 18
Solution model of the intrinsically disordered polyglutamine tract-binding protein-1. Biophys J 102(7):1608-16 (2012)
...Chen YW
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 51 nm3

SASDEE2 – The N-terminal domain of estrogen receptor alpha

The N-terminal domain of estrogen receptor alpha experimental SAS data
CUSTOM IN-HOUSE model
Sample: The N-terminal domain of estrogen receptor alpha monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 0.05 mM TCEP, pH: 7.4
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source (NSLS-II) on 2017 Jun 12
A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain. Structure 27(2):229-240.e4 (2019)
...Chen Y, Agrawal P, Zheng W, Shi W, Jiang W, Yang L, Chance MR, Surewicz WK, Buck M, Yang S
RgGuinier 3.0 nm
Dmax 10.0 nm

SASDKF2 – Mixed-sequence DNA dimer (25 base pair DNA)

Mixed-sequence 25 base-paired DNA experimental SAS data
Mixed-sequence 25 base-paired DNA Kratky plot
Sample: Mixed-sequence 25 base-paired DNA dimer, 16 kDa DNA
Buffer: 1.0 mM MgCl2, 10 mM Na-MOPS and 20uM EDTA, pH: 7
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source (NSLS-II) on 2019 Jun 7
Sequence Dependent DNA Conformation in WAXS
Yen-Lin Chen
RgGuinier 2.0 nm
Dmax 7.8 nm
VolumePorod 17 nm3

SASDHG2 – 12 base-paired RNA double helix (RNA12) with 30 mM KCl - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 30 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.4 nm

SASDKG2 – AT-sequence DNA dimer (25 base pair DNA)

AT-sequence 25 base-paired DNA experimental SAS data
AT-sequence 25 base-paired DNA Kratky plot
Sample: AT-sequence 25 base-paired DNA dimer, 16 kDa DNA
Buffer: 1.0 mM MgCl2, 10 mM Na-MOPS and 20uM EDTA, pH: 7
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source (NSLS-II) on 2019 Jun 7
Sequence Dependent DNA Conformation in WAXS
Yen-Lin Chen
RgGuinier 2.1 nm
Dmax 8.0 nm
VolumePorod 16 nm3

SASDHH2 – 12 base-paired RNA double helix (RNA12) with 50 mM KCl - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 50 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.4 nm

SASDHJ2 – 12 base-paired RNA double helix (RNA12) with 100 mM KCl - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 100 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.5 nm

SASDHK2 – 12 base-paired RNA double helix (RNA12) with 200 mM KCl - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 200 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.6 nm

SASDHL2 – 12 base-paired RNA double helix (RNA12) with 500 mM KCl - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 500 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 2.1 nm

SASDHM2 – 12 base-paired RNA double helix (RNA12) with 0.25 mM MgCl2 - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 0.25 mM MgCl2, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.4 nm

SASDHN2 – 12 base-paired RNA double helix (RNA12) with 1 mM MgCl2 - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 1.0 mM MgCl2, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.6 nm

SASDHP2 – 12 base-paired RNA double helix (RNA12) with 5 mM MgCl2 - SWAXS

12 base-paired RNA double helix experimental SAS data
12 base-paired RNA double helix Kratky plot
Sample: 12 base-paired RNA double helix monomer, 8 kDa RNA
Buffer: 5.0 mM MgCl2, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 2.0 nm

SASDHQ2 – 25 base-paired RNA double helix (RNA25) with 100 mM NaCl - WAXS

25 base-paired RNA double helix experimental SAS data
25 base-paired RNA double helix Kratky plot
Sample: 25 base-paired RNA double helix monomer, 16 kDa RNA
Buffer: 100 mM NaCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 May 13
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 2.1 nm

SASDHR2 – 25 base-paired RNA double helix (RNA25) with 10 mM MgCl2 - WAXS

25 base-paired RNA double helix experimental SAS data
25 base-paired RNA double helix Kratky plot
Sample: 25 base-paired RNA double helix monomer, 16 kDa RNA
Buffer: 10.0 mM MgCl2, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 May 13
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 2.6 nm

SASDHS2 – 25 base-paired RNA double helix (RNA25) with 400 mM KCl - WAXS

25 base-paired RNA double helix experimental SAS data
25 base-paired RNA double helix Kratky plot
Sample: 25 base-paired RNA double helix monomer, 16 kDa RNA
Buffer: 400 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 May 13
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 2.3 nm

SASDHT2 – 25 base-paired DNA double helix (DNA25) with 400 mM KCl - SWAXS

25 base-paired DNA double helix experimental SAS data
25 base-paired DNA double helix Kratky plot
Sample: 25 base-paired DNA double helix monomer, 15 kDa DNA
Buffer: 400 mM KCl, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.9 nm

SASDHU2 – 25 base-paired DNA double helix (DNA25) with 0.5 mM MgCl2 - SWAXS

25 base-paired DNA double helix experimental SAS data
25 base-paired DNA double helix Kratky plot
Sample: 25 base-paired DNA double helix monomer, 15 kDa DNA
Buffer: 0.5 mM MgCl2, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 2.0 nm

SASDHV2 – 25 base-paired DNA double helix (DNA25) with 2 mM MgCl2 - SWAXS

25 base-paired DNA double helix experimental SAS data
25 base-paired DNA double helix Kratky plot
Sample: 25 base-paired DNA double helix monomer, 15 kDa DNA
Buffer: 2.0 mM MgCl2, 20 mM KMOPS, 20 µM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 16
Salt Dependence of A-Form RNA Duplexes: Structures and Implications. J Phys Chem B 123(46):9773-9785 (2019)
Chen YL, Pollack L
RgGuinier 1.9 nm

SASDBL3 – Highly similar to Actin cross-linking family protein 7 (ACF7) Homo Sapiens

cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 experimental SAS data
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Kratky plot
Sample: cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 monomer, 46 kDa Homo sapiens protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at 12ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Nov 10
In vivo epidermal migration requires focal adhesion targeting of ACF7. Nat Commun 7:11692 (2016)
...Chen SY, Yang F, Liang H, Wu X
RgGuinier 3.4 nm
Dmax 13.5 nm
VolumePorod 53 nm3

SASDBN3 – Highly similar to Actin cross-linking family protein 7 (ACF7) Y259D mutant Homo Sapiens

cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant experimental SAS data
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant Kratky plot
Sample: cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant monomer, 46 kDa Homo sapiens protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at 12ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Nov 7
In vivo epidermal migration requires focal adhesion targeting of ACF7. Nat Commun 7:11692 (2016)
...Chen SY, Yang F, Liang H, Wu X
RgGuinier 3.4 nm
Dmax 13.5 nm
VolumePorod 55 nm3

SASDG54 – Human macrophage mannose receptor 1 protein

Macrophage mannose receptor 1 experimental SAS data
ITASSER model
Sample: Macrophage mannose receptor 1 dimer, 315 kDa Mouse myeloma cell … protein
Buffer: 50mM Hepes, 100mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at 12ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Apr 15
Mannose receptor (CD206) activation in tumor-associated macrophages enhances adaptive and innate antitumor immune responses. Sci Transl Med 12(530) (2020)
...Chen V, Ghebremedhin A, Karanam B, Bin Salam A, Amin R, Odzorig T, Aiken T, Nguyen V, Bian Y, Zarif JC, de Groot AE, Mehta M, Fan L, Hu X, Simeonov A, Pate N, Abu-Asab M, Ferrer M, Southall N, Ock CY,...
RgGuinier 7.9 nm
Dmax 30.1 nm
VolumePorod 584 nm3

SASDGD4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-381)

Retinoblastoma-binding protein 5Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2 experimental SAS data
Retinoblastoma-binding protein 5 Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Kratky plot
Sample: Retinoblastoma-binding protein 5 monomer, 42 kDa Homo sapiens protein
Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
...Chen Y
RgGuinier 5.7 nm
Dmax 18.6 nm
VolumePorod 360 nm3

SASDGE4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-480)

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 53 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
...Chen Y
RgGuinier 5.0 nm
Dmax 15.3 nm
VolumePorod 256 nm3

SASDGF4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-480)L399A/L400A/I457A/L459A

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 53 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
...Chen Y
RgGuinier 5.3 nm
Dmax 17.2 nm
VolumePorod 313 nm3

SASDGG4 – Mixed lineage leukemia protein-1 complex, MLL1-WDR5-ASH2L-RBBP5(2-538)

Histone-lysine N-methyltransferase 2AWD repeat-containing protein 5Set1/Ash2 histone methyltransferase complex subunit ASH2Retinoblastoma-binding protein 5 experimental SAS data
Histone-lysine N-methyltransferase 2A WD repeat-containing protein 5 Set1/Ash2 histone methyltransferase complex subunit ASH2 Retinoblastoma-binding protein 5 Kratky plot
Sample: Histone-lysine N-methyltransferase 2A monomer, 25 kDa Homo sapiens protein
WD repeat-containing protein 5 monomer, 34 kDa Homo sapiens protein
Set1/Ash2 histone methyltransferase complex subunit ASH2 monomer, 60 kDa Homo sapiens protein
Retinoblastoma-binding protein 5 monomer, 59 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 25mM Tris-HCl, 4% glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2019 Jun 22
The internal interaction in RBBP5 regulates assembly and activity of MLL1 methyltransferase complex. Nucleic Acids Res (2019)
...Chen Y
RgGuinier 5.0 nm
Dmax 15.5 nm
VolumePorod 282 nm3

SASDDX4 – Wild-type Protein sex-lethal

Protein sex-lethal experimental SAS data
Protein sex-lethal Kratky plot
Sample: Protein sex-lethal monomer, 20 kDa Drosophila melanogaster protein
Buffer: 10 mM KP, 50 mM NaCl, 10 mM DTT, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Oct 16
A General Small-Angle X-ray Scattering-Based Screening Protocol Validated for Protein-RNA Interactions. ACS Comb Sci 20(4):197-202 (2018)
Chen PC, Masiewicz P, Rybin V, Svergun D, Hennig J
RgGuinier 2.0 nm
Dmax 6.9 nm
VolumePorod 26 nm3

SASDDY4 – Protein sex-lethal mutant with 10GS-linker

Protein sex-lethal mutant experimental SAS data
Protein sex-lethal mutant with 10GS-linker Rg histogram
Sample: Protein sex-lethal mutant monomer, 20 kDa Drosophila melanogaster protein
Buffer: 10 mM KP, 50 mM NaCl, 10 mM DTT, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 2
A General Small-Angle X-ray Scattering-Based Screening Protocol Validated for Protein-RNA Interactions. ACS Comb Sci 20(4):197-202 (2018)
Chen PC, Masiewicz P, Rybin V, Svergun D, Hennig J
RgGuinier 2.1 nm
Dmax 7.4 nm
VolumePorod 27 nm3

SASDDZ4 – 1:1 Mixture between Protein sex-lethal mutant (Sxl10GS) and RNA decaneucleotide U8GU

Protein sex-lethal mutantRNA decaneucleotide U8GU experimental SAS data
1:1 Mixture between Protein sex-lethal mutant (Sxl10GS) and RNA decaneucleotide U8GU Rg histogram
Sample: Protein sex-lethal mutant monomer, 20 kDa Drosophila melanogaster protein
RNA decaneucleotide U8GU monomer, 3 kDa synthetic construct RNA
Buffer: 50% dilution of protein buffer {10 mM KP, 50 mM NaCl, 10 mM DTT pH 6} with {milliQ-water pH 7} suspended RNA, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 3
A General Small-Angle X-ray Scattering-Based Screening Protocol Validated for Protein-RNA Interactions. ACS Comb Sci 20(4):197-202 (2018)
Chen PC, Masiewicz P, Rybin V, Svergun D, Hennig J
RgGuinier 2.2 nm
Dmax 7.8 nm
VolumePorod 34 nm3

SASDD25 – 1:1 Mixture between Protein sex-lethal mutant (Sxl10GS) and RNA decaneucleotide UGU8

Protein sex-lethal mutantRNA decaneucleotide UGU8 experimental SAS data
1:1 Mixture between Protein sex-lethal mutant (Sxl10GS) and RNA decaneucleotide UGU8 Rg histogram
Sample: Protein sex-lethal mutant dimer, 41 kDa Drosophila melanogaster protein
RNA decaneucleotide UGU8 dimer, 6 kDa synthetic construct RNA
Buffer: 50% dilution of protein buffer {10 mM KP, 50 mM NaCl, 10 mM DTT pH 6} with {milliQ-water pH 7} suspended RNA, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2017 Apr 12
A General Small-Angle X-ray Scattering-Based Screening Protocol Validated for Protein-RNA Interactions. ACS Comb Sci 20(4):197-202 (2018)
Chen PC, Masiewicz P, Rybin V, Svergun D, Hennig J
RgGuinier 2.5 nm
Dmax 8.9 nm
VolumePorod 41 nm3

SASDA85 – CHD4 (PP-CC-AH-D)

Human Chromatin Remodeler CHD4 (363-1353) experimental SAS data
DAMMIF model
Sample: Human Chromatin Remodeler CHD4 (363-1353) monomer, 117 kDa Homo sapiens protein
Buffer: 50 mM HEPES 5% Glycerol 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2010 Nov 13
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
...Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED
RgGuinier 4.9 nm
Dmax 17.4 nm

SASDA95 – CHD4 (CC-AH-D)

Human Chromatin Remodeler CHD4 (494-1353) experimental SAS data
DAMMIF model
Sample: Human Chromatin Remodeler CHD4 (494-1353) monomer, 101 kDa Homo sapiens protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2010 Nov 13
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
...Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED
RgGuinier 4.0 nm
Dmax 14.5 nm

SASDAA5 – CHD4 (AH)

Human Chromatin Remodeler CHD4 (685-1233) experimental SAS data
DAMMIF model
Sample: Human Chromatin Remodeler CHD4 (685-1233) monomer, 63 kDa Homo sapiens protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2010 Nov 13
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
...Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED
RgGuinier 4.0 nm
Dmax 14.5 nm

SASDAB5 – CHD4 (PP-CC)

Human Chromatin Remodeler CHD4 (363-682) experimental SAS data
DAMMIF model
Sample: Human Chromatin Remodeler CHD4 (363-682) monomer, 38 kDa Homo sapiens protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2010 Nov 13
The PHD and chromo domains regulate the ATPase activity of the human chromatin remodeler CHD4. J Mol Biol 422(1):3-17 (2012)
...Chen Y, Burgess-Brown NA, Kouzarides T, Wiechens N, Owen-Hughes T, Svergun DI, Gileadi O, Laue ED
RgGuinier 3.0 nm
Dmax 10.5 nm

SASDD66 – Phox homologue (PX) - C2 domains of human phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (PI3KC2α)

Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha experimental SAS data
DAMFILT model
Sample: Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha monomer, 33 kDa Homo sapiens protein
Buffer: 25 mM Tris 200 mM NaCl 5% Glycerol 0.5 mM TCEP, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 20
Molecular Basis for Membrane Recruitment by the PX and C2 Domains of Class II Phosphoinositide 3-Kinase-C2α. Structure (2018)
Chen KE, Tillu VA, Chandra M, Collins BM
RgGuinier 2.6 nm
Dmax 9.3 nm
VolumePorod 43 nm3

SASDD76 – Phox Homologue (PX) - C2 domains of human phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha (PI3KC2α) in complex with inositol-hexaphosphate (IP6)

Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha experimental SAS data
DAMFILT model
Sample: Phox Homology (PX) - C2 domains of human Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha monomer, 33 kDa Homo sapiens protein
Buffer: 25 mM Tris 200 mM NaCl 5% Glycerol 0.5 mM TCEP 4 mM InsP6, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 20
Molecular Basis for Membrane Recruitment by the PX and C2 Domains of Class II Phosphoinositide 3-Kinase-C2α. Structure (2018)
Chen KE, Tillu VA, Chandra M, Collins BM
RgGuinier 2.6 nm
Dmax 9.3 nm
VolumePorod 48 nm3

SASDB86 – apo-BRD4

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 12
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
...Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti...
RgGuinier 7.0 nm
Dmax 27.0 nm

SASDB96 – Compound 1:BRD4 (1:1)

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 12
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
...Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti...
RgGuinier 6.2 nm
Dmax 27.5 nm

SASDBA6 – Compound 1:BRD4 (2:1)

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 12
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
...Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti...
RgGuinier 6.3 nm
Dmax 24.5 nm

SASDBB6 – Compound 6:BRD4 (1:1)

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2015 Feb 8
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
...Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti...
RgGuinier 5.1 nm
Dmax 24.3 nm

SASDBC6 – Compound 6:BRD4 (2:1)

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2015 Feb 8
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
...Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J, Petteruti...
RgGuinier 4.4 nm
Dmax 17.3 nm

SASDHC6 – C-terminal domain-like carotenoid protein (CCP2), apo-dimer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein dimer, 33 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
...Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 2.5 nm
Dmax 9.1 nm
VolumePorod 55 nm3

SASDHD6 – C-terminal domain-like carotenoid protein (CCP2), holo-dimer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein dimer, 36 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
...Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 2.5 nm
Dmax 7.9 nm
VolumePorod 62 nm3

SASDHE6 – C-terminal domain-like carotenoid protein (CCP2), apo-tetramer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein tetramer, 66 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
...Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 3.2 nm
Dmax 10.0 nm
VolumePorod 110 nm3

SASDHF6 – C-terminal domain-like carotenoid protein (CCP2), holo-tetramer

C-terminal domain-like carotenoid protein experimental SAS data
BILBOMD model
Sample: C-terminal domain-like carotenoid protein tetramer, 73 kDa Tolypothrix sp. PCC … protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 15
Structural analysis of a new carotenoid-binding protein: the C-terminal domain homolog of the OCP Scientific Reports 10(1) (2020)
...Chen Y, Petzold C, Ralston C, Polívka T, Kerfeld C
RgGuinier 3.3 nm
Dmax 12.1 nm
VolumePorod 157 nm3

SASDET6 – Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7)

Polyglutamine-binding protein 1 p.Lys192Serfs*7 experimental SAS data
Polyglutamine-binding protein 1 p.Lys192Serfs*7 (PQBP-1 XLID mutant K192Sfs*7) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Lys192Serfs*7 dimer, 47 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
...Chen YW
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 114 nm3

SASDEU6 – Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41)

Polyglutamine-binding protein 1 p.Arg153Serfs*41 experimental SAS data
Polyglutamine-binding protein 1 p.Arg153Serfs*41 (PQBP-1 XLID mutant R153Sfs*41) Rg histogram
Sample: Polyglutamine-binding protein 1 p.Arg153Serfs*41 dimer, 44 kDa Homo sapiens protein
Buffer: Phosphate-buffered saline, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III on 2013 Feb 15
Frameshift PQBP-1 mutants K192Sfs*7 and R153Sfs*41 implicated in X-linked intellectual disability form stable dimers. J Struct Biol (2019)
...Chen YW
RgGuinier 3.6 nm
Dmax 13.0 nm
VolumePorod 100 nm3

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
Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B Heterodimer Nucleasome Core Particle with Widom 601 DNA - HISTONE H3-H4 Heterodimer Nucleasome Core Particle with Widom 601 DNA - dsDNA Kratky plot
Sample: Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B Heterodimer dimer, 48 kDa Xenopus laevis protein
Nucleasome Core Particle with Widom 601 DNA - 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
Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the 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
RgGuinier 5.8 nm

SASDBT7 – Nucleosome Core Particle: 1.9 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
Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B Heterodimer Nucleasome Core Particle with Widom 601 DNA - HISTONE H3-H4 Heterodimer Nucleasome Core Particle with Widom 601 DNA - dsDNA Kratky plot
Sample: Nucleasome Core Particle with Widom 601 DNA - HISTONE H2A-H2B Heterodimer dimer, 48 kDa Xenopus laevis protein
Nucleasome Core Particle with Widom 601 DNA - 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
Asymmetric unwrapping of nucleosomal DNA propagates asymmetric opening and dissociation of the 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
RgGuinier 6.8 nm

SASDJV7 – pri-miR16-1 primary microRNA

primary microRNA pri-miR16-1 experimental SAS data
DAMMIF model
Sample: primary microRNA pri-miR16-1 monomer, 36 kDa Homo sapiens RNA
Buffer: 50 mM KCl, 50 mM HEPES, 5 mM DTT, 1% glycerol, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 12
Elucidating the Role of Microprocessor Protein DGCR8 in Bending RNA Structures Biophysical Journal (2020)
...Chen Y, Usher E, Cook E, Pollack L, Showalter S
RgGuinier 4.4 nm
Dmax 17.2 nm
VolumePorod 74 nm3

SASDJW7 – pri-miR16-1 primary microRNA in complex with DGCR8-core protein

primary microRNA pri-miR16-1 complexed with DGCR8-core proteinMicroprocessor complex subunit DGCR8 experimental SAS data
DAMMIF model
Sample: primary microRNA pri-miR16-1 complexed with DGCR8-core protein monomer, 36 kDa Homo sapiens RNA
Microprocessor complex subunit DGCR8 monomer, 26 kDa Homo sapiens protein
Buffer: 50 mM KCl, 50 mM HEPES, 5 mM DTT, 1% glycerol, 50% sucrose, DGCR8-core, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Apr 12
Elucidating the Role of Microprocessor Protein DGCR8 in Bending RNA Structures Biophysical Journal (2020)
...Chen Y, Usher E, Cook E, Pollack L, Showalter S
RgGuinier 5.0 nm
Dmax 17.2 nm
VolumePorod 125 nm3

SASDA28 – anti-TG2 antibody (679 14 E06)

anti-TG2 antibody (679 14 E06)  experimental SAS data
CRYSOL model
Sample: anti-TG2 antibody (679 14 E06) monomer, 48 kDa protein
Buffer: 20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM
RgGuinier 2.5 nm
Dmax 8.1 nm
VolumePorod 58 nm3

SASDA38 – transglutaminase-2 (TGA2)

transglutaminase 2 experimental SAS data
CRYSOL model
Sample: transglutaminase 2 monomer, 79 kDa Homo sapiens protein
Buffer: 20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 117 nm3

SASDA48 – transglutaminase2:anti-transglutaminase2 FAB1 antibody complex

anti-TG2 antibody (679 14 E06) transglutaminase 2 experimental SAS data
DAMMIN model
Sample: anti-TG2 antibody (679 14 E06) monomer, 48 kDa protein
transglutaminase 2 monomer, 79 kDa Homo sapiens protein
Buffer: 20 mM Tris 150mM NaCl 1mM EDTA, pH: 7.2
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jan 17
Structural Basis for Antigen Recognition by Transglutaminase 2-specific Autoantibodies in Celiac Disease. J Biol Chem 290(35):21365-75 (2015)
Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM
RgGuinier 4.0 nm
Dmax 13.9 nm
VolumePorod 168 nm3

SASDFD8 – Histidine-binding periplasmic protein (HisBP), apo-form

Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.0 nm
Dmax 6.0 nm
VolumePorod 32 nm3

SASDFE8 – Histidine-binding periplasmic protein (HisBP) in the presence of histidine - His-bound 5-fold excess

Histidine-binding periplasmic protein experimental SAS data
Histidine-binding periplasmic protein Kratky plot
Sample: Histidine-binding periplasmic protein monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 1.8 nm
Dmax 5.7 nm
VolumePorod 33 nm3

SASDFF8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP), apo-form

Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.2 nm
VolumePorod 35 nm3

SASDFG8 – Glutamine-binding periplasmic protein with hexahistidine tag (GlnBP) in the presence of glutamine - Gln-bound 10-fold excess

Glutamine-binding periplasmic protein with hexahistidine tag experimental SAS data
Glutamine-binding periplasmic protein with hexahistidine tag Kratky plot
Sample: Glutamine-binding periplasmic protein with hexahistidine tag monomer, 26 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.0 nm
Dmax 6.1 nm
VolumePorod 34 nm3

SASDFH8 – Glutamate/aspartate import solute-binding protein (DEBP), apo-form

Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.3 nm
Dmax 8.5 nm
VolumePorod 44 nm3

SASDFJ8 – Glutamate/aspartate import solute-binding protein (DEBP) in the presence of glutamate - Glu-bound 10-fold excess

Glutamate/aspartate import solute-binding protein experimental SAS data
Glutamate/aspartate import solute-binding protein Kratky plot
Sample: Glutamate/aspartate import solute-binding protein monomer, 32 kDa Escherichia coli protein
Buffer: 100 mM NaCl, 20 mM NaPO4, 0.5 mM TCEP, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 10
Structure-based screening of binding affinities via small-angle X-ray scattering (2019)
Chen P, Masiewicz P, Perez K, Hennig J
RgGuinier 2.1 nm
Dmax 6.4 nm
VolumePorod 39 nm3

SASDHJ8 – ACT domain of the Mycobacterium tuberculosis Rel protein

ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) experimental SAS data
ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) Kratky plot
Sample: ACT domain of Rel protein (Bifunctional (p)ppGpp synthase/hydrolase RelA) dimer, 20 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl, 350 mM NaCl, 5% glycerol, 1 mM DTT, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar, Nanyang Technological University on 2018 Jun 7
Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein. FEBS J (2020)
...Chen MW, Ragunathan P, Grüber G
RgGuinier 1.9 nm
Dmax 6.1 nm
VolumePorod 29 nm3

SASDDU8 – Multidomain architecture of the estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains

Estrogen receptorERE1ERE2EstradiolhERa peptide1hERa peptide2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Estrogen receptor dimer, 85 kDa protein
ERE1 monomer, 6 kDa Homo sapiens DNA
ERE2 monomer, 6 kDa Homo sapiens DNA
Estradiol dimer, 0 kDa
hERa peptide1 monomer, 2 kDa protein
hERa peptide2 monomer, 2 kDa protein
Buffer: 10 mM CHES (pH9.5), 125 mM NaCl, 5mM KCl, 4 mM MgCl2, 50 mM arginine, 50 mM glutamate, 5 mM TCEP, 5% glycerol, 10 µm Zn acetate, 10 µM estradiol, pH: 9.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Aug 10
Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains. Nat Commun 9(1):3520 (2018)
...Chen Y, Chakravarthy S, Gupta S, Ralston C, Kao HY, Chance MR, Yang S
RgGuinier 3.8 nm
Dmax 11.5 nm

SASDCH9 – Bifunctional enzyme responsible for the synthesis and hydrolysis of c-di-GMP (DcpA) with GDP

Sensory box/response regulator experimental SAS data
CORAL model
Sample: Sensory box/response regulator dimer, 136 kDa Mycobacterium smegmatis (strain … protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5% glycerol, 2 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Jun 26
The GDP-switched GAF domain of DcpA modulates the concerted synthesis/hydrolysis of c-di-GMP in Mycobacterium smegmatis. Biochem J 475(7):1295-1308 (2018)
Chen HJ, Li N, Luo Y, Jiang YL, Zhou CZ, Chen Y, Li Q
RgGuinier 5.0 nm
Dmax 20.0 nm
VolumePorod 299 nm3

SASDCJ9 – Bifunctional enzyme responsible for the synthesis and hydrolysis of c-di-GMP (DcpA) without GDP

Sensory box/response regulator experimental SAS data
CORAL model
Sample: Sensory box/response regulator dimer, 136 kDa Mycobacterium smegmatis (strain … protein
Buffer: 20 mM HEPES, 100 mM NaCl, 5% glycerol, 2 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Jun 26
The GDP-switched GAF domain of DcpA modulates the concerted synthesis/hydrolysis of c-di-GMP in Mycobacterium smegmatis. Biochem J 475(7):1295-1308 (2018)
Chen HJ, Li N, Luo Y, Jiang YL, Zhou CZ, Chen Y, Li Q
RgGuinier 4.8 nm
Dmax 17.0 nm
VolumePorod 271 nm3

SASDFR6 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (ratio DNA:Protein 1:1)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 228 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jul 8
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.1 nm
Dmax 21.9 nm
VolumePorod 251 nm3

SASDFS6 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (ratio DNA:Protein 1:2.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 267 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jul 8
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.0 nm
Dmax 25.0 nm
VolumePorod 386 nm3

SASDFT6 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (ratio DNA:Protein 1:5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 267 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jul 8
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.2 nm
Dmax 27.0 nm
VolumePorod 474 nm3

SASDFU6 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (ratio DNA:Protein 1:10)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 305 kDa Escherichia coli protein
Buffer: 20mM HEPES, 100mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jul 8
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 8.0 nm
Dmax 24.8 nm
VolumePorod 448 nm3

SASDFN6 – DNA-binding protein HU-alpha

DNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha octamer, 77 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 3.2 nm
Dmax 10.7 nm

SASDFP6 – 80 base pair DNA

80bp_DNA Forward80bp_DNA Reverse experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.0 nm
Dmax 28.9 nm

SASDF36 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 50 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM sodium acetate, 50 mM NaCl, pH: 4.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDF46 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 100 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM sodium acetate, 100 mM NaCl, pH: 4.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDF56 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 150 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM sodium acetate, 150 mM NaCl, pH: 4.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDF66 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 4.5 with 300 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM sodium acetate, 300 mM NaCl, pH: 4.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDFX5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 5.5 with 50 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 50 mM NaCl, pH: 5.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDFY5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 5.5 with 100 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 5.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDFZ5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 5.5 with 150 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 150 mM NaCl, pH: 5.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDF26 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 5.5 with 300 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha decamer, 95 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 300 mM NaCl, pH: 5.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.4 nm
Dmax 24.4 nm
VolumePorod 268 nm3

SASDFT5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 6.5 with 50 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha , 10 kDa Escherichia coli protein
Buffer: 10mM Bis-Tris, 50 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDFU5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 6.5 with 100 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 14-mer, 133 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.2 nm
Dmax 24.4 nm
VolumePorod 274 nm3

SASDFV5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 6.5 with 150 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 14-mer, 133 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 150 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.0 nm
Dmax 26.2 nm
VolumePorod 352 nm3

SASDFW5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 6.5 with 300 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha decamer, 95 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 300 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.0 nm
Dmax 24.7 nm
VolumePorod 218 nm3

SASDFP5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 50 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 16-mer, 153 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 27
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 8.9 nm
Dmax 28.5 nm
VolumePorod 410 nm3

SASDFQ5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 100 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 16-mer, 153 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.6 nm
Dmax 25.0 nm
VolumePorod 336 nm3

SASDFR5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 150 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha 14-mer, 133 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 5.8 nm
Dmax 24.2 nm
VolumePorod 308 nm3

SASDFS5 – DNA-binding protein HU-alpha bound to 80 base-pair DNA at pH 7.5 with 300 mM NaCl

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha decamer, 95 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 6.5 nm
Dmax 24.0 nm
VolumePorod 242 nm3

SASDFQ6 – DNA-binding protein HU-alpha, E34K

DNA-binding protein HU-alpha, E34K experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha, E34K dimer, 19 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 1
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 2.2 nm
Dmax 6.7 nm
VolumePorod 36 nm3

SASDGB3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 4.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K dimer, 19 kDa Escherichia coli protein
Buffer: 10 mM sodium acetate, 50 mM NaCl, pH: 4.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDGC3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 5.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K dimer, 19 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 50 mM NaCl, pH: 5.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M

SASDGD3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 6.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 100 kDa Escherichia coli protein
Buffer: 10mM Bis-Tris, 50 mM NaCl, pH: 6.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.3 nm
Dmax 28.0 nm
VolumePorod 330 nm3

SASDGE3 – DNA-binding protein HU-alpha, E34K mutant bound to 80 bp DNA (pH 7.5)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E34K experimental SAS data
80bp_DNA Forward 80bp_DNA Reverse DNA-binding protein HU-alpha, E34K Kratky plot
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E34K , 100 kDa Escherichia coli protein
Buffer: 10 mM Bis-Tris, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 2
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling. Nat Commun 11(1):2905 (2020)
...Chen JH, Ekman AA, Larabell CA, Adhya S, Hammel M
RgGuinier 7.1 nm
Dmax 27.5 nm
VolumePorod 309 nm3