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254 hits found for Nucleic Acids Res

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)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 22 nm3

SASDJ52 – DNA repair protein XRCC1ΔN monomer/dimer

DNA repair protein XRCC1ΔN experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1ΔN dimer, 76 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Jul 15
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 170 nm3

SASDC62 – Basic domain of telomeric repeat-binding factor 2 (TRF2)

Basic domain of telomeric repeat-binding factor 2 experimental SAS data
Basic domain of telomeric repeat-binding factor 2 Kratky plot
Sample: Basic domain of telomeric repeat-binding factor 2 monomer, 5 kDa Homo sapiens protein
Buffer: 50 mM NaPi, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2015 Mar 5
...restores it. Nucleic Acids Res 45(21):12170-12180 (2017)
Necasová I, Janoušková E, Klumpler T, Hofr C
RgGuinier 1.7 nm
Dmax 7.1 nm
VolumePorod 4 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)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 3.1 nm
Dmax 13.3 nm
VolumePorod 25 nm3

SASDJ62 – DNA repair protein XRCC1 monomer /dimer

DNA repair protein XRCC1 experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1 , 69 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 19
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.3 nm
Dmax 26.9 nm
VolumePorod 330 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)
Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J
RgGuinier 1.8 nm
Dmax 8.5 nm
VolumePorod 14 nm3

SASDJ72 – DNA Ligase IIIα monomer/dimer

DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: DNA ligase 3 (DNA ligase III alpha) , Homo sapiens protein
Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl, 10% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2011 Mar 31
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.1 nm
Dmax 21.0 nm
VolumePorod 240 nm3

SASDJ82 – DNA repair protein XRCC1 - DNA Ligase IIIα complex

DNA repair protein XRCC1DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: DNA repair protein XRCC1 , 69 kDa Homo sapiens protein
DNA ligase 3 (DNA ligase III alpha) , Homo sapiens protein
Buffer: 50 mM Tris-HCl, pH 7.5, 100 mM NaCl, 5 mM MgCl₂,  0.2 mM PMSF, 1 mM benzamidine, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Aug 18
An atypical BRCT-BRCT interaction with the XRCC1 scaffold protein compacts human DNA Ligase IIIα within a flexible DNA repair complex. Nucleic Acids Res (2020)
Hammel M, Rashid I, Sverzhinsky A, Pourfarjam Y, Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.2 nm
Dmax 27.9 nm
VolumePorod 675 nm3

SASDK92 – ...acids 215-619

Interferon-activable protein 204 experimental SAS data
CHIMERA model
Sample: Interferon-activable protein 204 monomer, 47 kDa Mus musculus protein
Buffer: 20 mM HEPES, 100 mM KCl, pH: 7.4
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2013 Mar 14
Structural mechanism of DNA recognition by the p204 HIN domain. Nucleic Acids Res (2021)
Fan X, Jiang J, Zhao D, Chen F, Ma H, Smith P, Unterholzner L, Xiao TS, Jin T
RgGuinier 3.1 nm
Dmax 9.5 nm
VolumePorod 28 nm3

SASDJB2Restriction endonuclease R.AgeI in apo form, monomeric

Type-2 restriction enzyme AgeI experimental SAS data
DAMMIN model
Sample: ...restriction enzyme AgeI monomer, 31 kDa Thalassobius gelatinovorus protein
Buffer: 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl₂, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 14
Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA. Nucleic Acids Res 45(6):3547-3558 (2017)
Tamulaitiene G, Jovaisaite V, Tamulaitis G, Songailiene I, Manakova E, Zaremba M, Grazulis S, Xu SY, Siksnys V
RgGuinier 2.2 nm
Dmax 6.7 nm
VolumePorod 53 nm3

SASDJC2Restriction endonuclease R.AgeI complex with cognate DNA

Type-2 restriction enzyme AgeICognate DNA oligoduplex with 5'-T overhang experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: ...restriction enzyme AgeI dimer, 61 kDa Thalassobius gelatinovorus protein
Cognate DNA oligoduplex with 5'-T overhang dimer, 8 kDa DNA
Buffer: 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaCl₂, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Nov 14
Restriction endonuclease AgeI is a monomer which dimerizes to cleave DNA. Nucleic Acids Res 45(6):3547-3558 (2017)
Tamulaitiene G, Jovaisaite V, Tamulaitis G, Songailiene I, Manakova E, Zaremba M, Grazulis S, Xu SY, Siksnys V
RgGuinier 2.4 nm
Dmax 7.4 nm
VolumePorod 69 nm3

SASDJW2 – ...restriction endonuclease

5-methylcytosine-specific restriction enzyme A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: ...restriction enzyme A dimer, 65 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 95 nm3

SASDJX2 – ...restriction endonuclease in complex with cognate hemimethylated 12bp oligoduplex

cognate hemimethylated 12-bp oligoduplex5-methylcytosine-specific restriction enzyme A experimental SAS data
SASREF model
Sample: cognate hemimethylated 12-bp oligoduplex dimer, 15 kDa DNA
...restriction enzyme A dimer, 65 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 3.9 nm
Dmax 13.5 nm
VolumePorod 69 nm3

SASDJY2 – ...restriction endonuclease

5-methylcytosine-specific restriction enzyme A (N-terminal domain) experimental SAS data
OTHER model
Sample: ...restriction enzyme A (N-terminal domain) monomer, 21 kDa Escherichia coli protein
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 29 nm3

SASDJZ2 – ...restriction endonuclease in complex with cognate hemimethylated 12bp oligoduplex

5-methylcytosine-specific restriction enzyme A (N-terminal domain)cognate hemimethylated 12-bp oligoduplex experimental SAS data
OTHER model
Sample: ...restriction enzyme A (N-terminal domain) monomer, 21 kDa Escherichia coli protein
cognate hemimethylated 12-bp oligoduplex monomer, 7 kDa DNA
Buffer: 20 mM Tris–HCl pH 7.5, 200 mM KCl, 0.1 mM EDTA, 0.01% (w/v) sodium azide and 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 May 24
Activity and structure of EcoKMcrA. Nucleic Acids Res 46(18):9829-9841 (2018)
Czapinska H, Kowalska M, Zagorskaite E, Manakova E, Slyvka A, Xu SY, Siksnys V, Sasnauskas G, Bochtler M
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 29 nm3

SASDKF3 – Human telomere monomer G4 hybrid-2 form (2JSL)

Human telomere G-quadruplex hybrid-2 form experimental SAS data
DAMMIN model
Sample: Human telomere G-quadruplex hybrid-2 form monomer, 8 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Aug 14
...res of higher-order human telomere G-quadruplex multimers. Nucleic Acids Res (2021)
...res JB, Trent JO
RgGuinier 1.2 nm
Dmax 3.8 nm
VolumePorod 9 nm3

SASDKG3 – Human wild-type telomere 48-mer d(TTAGGG)8

Human Telomere Repeat (TTAGGG)8 experimental SAS data
DAMMIN model
Sample: Human Telomere Repeat (TTAGGG)8 monomer, 15 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Aug 14
...res of higher-order human telomere G-quadruplex multimers. Nucleic Acids Res (2021)
...res JB, Trent JO
RgGuinier 1.9 nm
Dmax 6.4 nm
VolumePorod 16 nm3

SASDKH3 – Human wild-type telomere 72mer d(TTAGGG)12

Human Telomere Repeat (TTAGGG)12 experimental SAS data
DAMMIF model
Sample: Human Telomere Repeat (TTAGGG)12 monomer, 23 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Aug 14
...res of higher-order human telomere G-quadruplex multimers. Nucleic Acids Res (2021)
...res JB, Trent JO
RgGuinier 2.5 nm
Dmax 8.7 nm
VolumePorod 26 nm3

SASDKJ3 – Human telomere DNA d(TTAGGG)96

Human Telomere 96mer experimental SAS data
DAMMIF model
Sample: Human Telomere 96mer monomer, 31 kDa synthetic construct DNA
Buffer: 6 mM Na2HPO4, 2 mM NaH2PO4, 1 mM Na2EDTA, 185 mM KCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Feb 19
...res of higher-order human telomere G-quadruplex multimers. Nucleic Acids Res (2021)
...res JB, Trent JO
RgGuinier 3.2 nm
Dmax 10.9 nm
VolumePorod 38 nm3

SASDAN3 – MutS dimer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS dimer, 191 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Feb 28
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 4.7 nm
Dmax 15.5 nm
VolumePorod 307 nm3

SASDAQ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 28.0 nm
VolumePorod 700 nm3

SASDDR3 – Yeast tRNA Nm34 methyltransferase Trm7-Trm734 complex from Sacharomyces cerevisiae

Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseTrm734: Regulator of Ty1 transposition protein 10 experimental SAS data
CORAL model
Sample: Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase monomer, 36 kDa Saccharomyces cerevisiae protein
Trm734: Regulator of Ty1 transposition protein 10 monomer, 116 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM HEPES, 200 mM KCl, 5% v/v Glycerol, 10mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BL-10C, ...Research Organization (KEK) on 2015 Dec 16
Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition. Nucleic Acids Res (2019)
Hirata A, Okada K, Yoshii K, Shiraishi H, Saijo S, Yonezawa K, Shimizu N, Hori H
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 218 nm3

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.5 nm
Dmax 29.0 nm
VolumePorod 750 nm3

SASDBX3 – Aureobox dsDNA

Aureobox dsDNA experimental SAS data
DAMFILT model
Sample: Aureobox dsDNA monomer, 13 kDa synthetic construct DNA
Buffer: 50 mM Tris 50 mM boric acid 1 mM EDTA, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 6
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 44(12):5957-70 (2016)
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 2.0 nm
Dmax 8.6 nm
VolumePorod 18 nm3

SASDAY3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.3 nm
Dmax 29.0 nm
VolumePorod 720 nm3

SASDBY3 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage) module (light state-TBE)

Aureochrome 1a bZIP-LOV module experimental SAS data
DAMFILT model
Sample: Aureochrome 1a bZIP-LOV module dimer, 57 kDa Phaeodactylum tricornutum protein
Buffer: 50 mM Tris 50 mM boric acid 1 mM EDTA, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 6
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 44(12):5957-70 (2016)
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 3.4 nm
Dmax 12.6 nm
VolumePorod 115 nm3

SASDAZ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.0 nm

SASDBZ3 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage)/DNA complex (light state)

Aureobox dsDNAAureochrome 1a bZIP-LOV module experimental SAS data
DAMFILT model
Sample: Aureobox dsDNA monomer, 13 kDa synthetic construct DNA
Aureochrome 1a bZIP-LOV module dimer, 57 kDa Phaeodactylum tricornutum protein
Buffer: 50 mM Tris 50 mM boric acid 1 mM EDTA, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 6
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 44(12):5957-70 (2016)
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 4.5 nm
Dmax 16.7 nm
VolumePorod 97 nm3

SASDA24 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 27.0 nm

SASDB24 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage) module (light state, Tris)

Aureochrome 1a bZIP-LOV module experimental SAS data
Aureochrome 1a bZIP-LOV module Kratky plot
Sample: Aureochrome 1a bZIP-LOV module dimer, 57 kDa Phaeodactylum tricornutum protein
Buffer: 10 mM Tris 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 6
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 44(12):5957-70 (2016)
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 3.9 nm
Dmax 12.5 nm
VolumePorod 121 nm3

SASDB34 – Aureochrome 1a bZIP-LOV module: PtAUREO1a bZIP-LOV (Light oxygen voltage) module (dark state, Tris)

Aureochrome 1a bZIP-LOV module experimental SAS data
Aureochrome 1a bZIP-LOV module Kratky plot
Sample: Aureochrome 1a bZIP-LOV module dimer, 57 kDa Phaeodactylum tricornutum protein
Buffer: 10 mM Tris 300 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 6
...responsive domains of diatom class I aureochromes. Nucleic Acids Res 44(12):5957-70 (2016)
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 117 nm3

SASDH44 – 3' Complex of XPA-DBD and RPA70AB

DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit3-prime  Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
3-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 17 Nov 2
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 3.1 nm
Dmax 9.7 nm
VolumePorod 103 nm3

SASDH54 – 5' Complex of XPA-DBD with RPA70AB

DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunit5-prime Nucleotide Excision Repair Junction Model Substrate experimental SAS data
HADDOCK model
Sample: DNA repair protein complementing XP-A cells monomer, 17 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 27 kDa Homo sapiens protein
5-prime Nucleotide Excision Repair Junction Model Substrate monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 4
A key interaction with RPA orients XPA in NER complexes. Nucleic Acids Res (2020)
Topolska-Woś AM, Sugitani N, Cordoba JJ, Le Meur KV, Le Meur RA, Kim HS, Yeo JE, Rosenberg D, Hammel M, Schärer OD, Chazin WJ
RgGuinier 2.9 nm
Dmax 97.0 nm
VolumePorod 87 nm3

SASDC74 – ...resolved 0ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.5 nm
Dmax 8.0 nm

SASDK74 – Streptococcus agalactiae transcription factor BusR - RCK_C domain

Transcriptional repressor BusR RCK_C domain experimental SAS data
OTHER model
Sample: ...ressor BusR RCK_C domain dimer, 22 kDa Streptococcus agalactiae serotype … protein
Buffer: 100 mM NaCl, 30mM Hepes, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 2
BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture. Nucleic Acids Res (2021)
Bandera AM, Bartho J, Lammens K, Drexler DJ, Kleinschwärzer J, Hopfner KP, Witte G
RgGuinier 1.9 nm
Dmax 6.4 nm
VolumePorod 44 nm3

SASDK84 – Streptococcus agalactiae transcription factor BusR

Transcriptional repressor BusR experimental SAS data
Transcriptional repressor BusR Kratky plot
Sample: ...ressor BusR tetramer, 95 kDa Streptococcus agalactiae protein
Buffer: 20mM HEPES, pH6.5, 100mM NaCl, 3% glycerol (v/v), pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 2
BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture. Nucleic Acids Res (2021)
Bandera AM, Bartho J, Lammens K, Drexler DJ, Kleinschwärzer J, Hopfner KP, Witte G
RgGuinier 4.4 nm
Dmax 13.9 nm
VolumePorod 168 nm3

SASDC94 – ...resolved 10ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.3 nm
Dmax 7.2 nm

SASDK94 – Streptococcus agalactiae transcription factor BusR dsDNA complex

Transcriptional repressor BusRBusR Recognition sequence experimental SAS data
OTHER model
Sample: ...ressor BusR tetramer, 95 kDa Streptococcus agalactiae protein
BusR Recognition sequence monomer, 28 kDa synthetic construct DNA
Buffer: 20mM HEPES, pH6.5, 100mM NaCl, 3% glycerol (v/v), pH: 6.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 2
BusR senses bipartite DNA binding motifs by a unique molecular ruler architecture. Nucleic Acids Res (2021)
Bandera AM, Bartho J, Lammens K, Drexler DJ, Kleinschwärzer J, Hopfner KP, Witte G
RgGuinier 4.3 nm
Dmax 14.2 nm
VolumePorod 210 nm3

SASDCA4 – ...resolved 30ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.2 nm
Dmax 7.0 nm

SASDCB4 – ...resolved 100ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.3 nm
Dmax 7.1 nm

SASDCC4 – ...resolved 300ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.2 nm
Dmax 6.8 nm

SASDCD4 – ...resolved 1000ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.2 nm
Dmax 6.8 nm

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)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.7 nm
Dmax 18.6 nm
VolumePorod 360 nm3

SASDCE4 – ...resolved 3000ms

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 10mM KMOPS 20mM KCl 1mM MgCl2 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Dec 3
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.2 nm
Dmax 6.7 nm

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)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.0 nm
Dmax 15.3 nm
VolumePorod 256 nm3

SASDCF4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 20mM KCl

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 20mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.6 nm
Dmax 8.5 nm

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)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.3 nm
Dmax 17.2 nm
VolumePorod 313 nm3

SASDCG4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 100mM KCl

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 100mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.5 nm
Dmax 8.0 nm

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)
Han J, Li T, Li Y, Li M, Wang X, Peng C, Su C, Li N, Li Y, Xu Y, Chen Y
RgGuinier 5.0 nm
Dmax 15.5 nm
VolumePorod 282 nm3

SASDCH4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 200mm KCl

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 200mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.5 nm
Dmax 8.0 nm

SASDCJ4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 400mM KCl

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 400mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.4 nm
Dmax 8.0 nm

SASDBK4 – The 1:1:3:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F short Cascade complex

short-crRNA: CRISPR/Cas Type I-F Cascade componentCas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) experimental SAS data
DAMMIF model
Sample: short-crRNA: CRISPR/Cas Type I-F Cascade component monomer, 14 kDa Shewanella putrefaciens RNA
Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, 21 kDa Shewanella putrefaciens protein
Trimeric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) trimer, 112 kDa Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, 38 kDa Shewanella putrefaciens protein
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Jun 27
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 44(12):5872-82 (2016)
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 4.1 nm
Dmax 14.2 nm

SASDCK4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 0.25mM MgCl2

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 20mM KCl 0.25mM MgCl2 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.4 nm
Dmax 7.6 nm

SASDBL4 – The 1:1:6:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F wild-type Cascade complex

Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)wildtype-crRNA: CRISPR/Cas Type I-F Cascade component experimental SAS data
DAMMIF model
Sample: Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, 21 kDa Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, 38 kDa Shewanella putrefaciens protein
Hexameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) hexamer, 223 kDa Shewanella putrefaciens protein
wildtype-crRNA: CRISPR/Cas Type I-F Cascade component monomer, 19 kDa RNA
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Jun 27
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 44(12):5872-82 (2016)
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 5.4 nm
Dmax 18.4 nm

SASDCL4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 0.50mM MgCl2

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 0.5mM MgCl2 20mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.3 nm
Dmax 7.2 nm

SASDBM4 – The 1:1:9:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F long Cascade complex

Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)long-crRNA: CRISPR/Cas Type I-F Cascade component experimental SAS data
DAMMIF model
Sample: Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, 21 kDa Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, 38 kDa Shewanella putrefaciens protein
Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) nonamer, 335 kDa Shewanella putrefaciens protein
long-crRNA: CRISPR/Cas Type I-F Cascade component monomer, 25 kDa RNA
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2016 Jan 30
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 44(12):5872-82 (2016)
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 6.5 nm
Dmax 21.6 nm

SASDCM4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 1mM MgCl2

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data
Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot
Sample: Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer: 1mM MgCl2 20mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17
Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L
RgGuinier 2.2 nm
Dmax 7.2 nm

SASDMM4 – Hepatitis C virus 5BSL3.2 RNA subdomain

5BSL3.2 experimental SAS data
DAMFILT model
Sample: 5BSL3.2 monomer, 15 kDa Hepatitis C virus … RNA
Buffer: 10 mM Tris-HCl, 0.1 mM EDTA, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2019 Jun 2
...resolution structural models of hepatitis C virus RNA subdomain 5BSL3.2 and its distal complex with domain 3'X point to conserved regulatory mechanisms within the Flaviviridae family. Nucleic Acids Res (2022)
Castillo-Martínez J, Fan L, Szewczyk MP, Wang YX, Gallego J
RgGuinier 2.5 nm
Dmax 7.6 nm
VolumePorod 29 nm3

SASDMN4 – Hepatitis C virus 5BSL3.2 RNA subdomain

5BSL3.2 experimental SAS data
DAMFILT model
Sample: 5BSL3.2 monomer, 15 kDa Hepatitis C virus … RNA
Buffer: 10 mM Tris-HCl, 6 mM MgCl2, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2019 Jun 2
...resolution structural models of hepatitis C virus RNA subdomain 5BSL3.2 and its distal complex with domain 3'X point to conserved regulatory mechanisms within the Flaviviridae family. Nucleic Acids Res (2022)
Castillo-Martínez J, Fan L, Szewczyk MP, Wang YX, Gallego J
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 22 nm3

SASDMP4 – Hepatitis C virus RNA Domain 3'X mutant

Domain 3'X mutant experimental SAS data
DAMFILT model
Sample: Domain 3'X mutant monomer, 32 kDa Hepatitis C virus … RNA
Buffer: 10 mM Tris-HCl, 0.1 mM EDTA, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2019 Jun 2
...resolution structural models of hepatitis C virus RNA subdomain 5BSL3.2 and its distal complex with domain 3'X point to conserved regulatory mechanisms within the Flaviviridae family. Nucleic Acids Res (2022)
Castillo-Martínez J, Fan L, Szewczyk MP, Wang YX, Gallego J
RgGuinier 4.1 nm
Dmax 14.7 nm
VolumePorod 70 nm3

SASDMQ4 – Hepatitis C virus RNA Domain 3'X mutant

Domain 3'X mutant experimental SAS data
DAMFILT model
Sample: Domain 3'X mutant monomer, 32 kDa Hepatitis C virus … RNA
Buffer: 10 mM Tris-HCl, 6 mM MgCl2, pH: 7
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jun 2
...resolution structural models of hepatitis C virus RNA subdomain 5BSL3.2 and its distal complex with domain 3'X point to conserved regulatory mechanisms within the Flaviviridae family. Nucleic Acids Res (2022)
Castillo-Martínez J, Fan L, Szewczyk MP, Wang YX, Gallego J
RgGuinier 3.3 nm
Dmax 14.2 nm
VolumePorod 50 nm3

SASDMR4 – Hepatitis C virus RNA Domain 3'X mutant - Subdomain 5BSL3.2 complex

Domain 3'X mutant - 5BSL3.2 complex experimental SAS data
DAMFILT model
Sample: Domain 3'X mutant - 5BSL3.2 complex monomer, 42 kDa Hepatitis C virus … RNA
Buffer: 10 mM Tris-HCl, 6 mM MgCl2, pH: 7
Experiment: SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2019 Jun 2
...resolution structural models of hepatitis C virus RNA subdomain 5BSL3.2 and its distal complex with domain 3'X point to conserved regulatory mechanisms within the Flaviviridae family. Nucleic Acids Res (2022)
Castillo-Martínez J, Fan L, Szewczyk MP, Wang YX, Gallego J
RgGuinier 4.2 nm
Dmax 17.0 nm
VolumePorod 88 nm3

SASDCY4 – RNase E 603-850

RNase E 603-850 experimental SAS data
RNase E 603-850 Rg histogram
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 5
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.3 nm
Dmax 27.5 nm
VolumePorod 139 nm3

SASDCZ4 – RNase E 603-850/ATP-dependent RNA helicase (RhlB) binary complex

RNase E 603-850ATP-dependent RNA helicase RhlB experimental SAS data
GASBOR model
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
ATP-dependent RNA helicase RhlB monomer, 47 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Feb 11
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.4 nm
Dmax 29.5 nm
VolumePorod 183 nm3

SASDC25 – RNase E 603-850/ATP-dependent RNA helicase (RhlB)/enolase ternary complex

RNase E 603-850ATP-dependent RNA helicase RhlBEnolase experimental SAS data
GASBOR model
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
ATP-dependent RNA helicase RhlB monomer, 47 kDa Escherichia coli protein
Enolase dimer, 91 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Jul 16
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 6.4 nm
Dmax 30.5 nm
VolumePorod 280 nm3

SASDL35 – Schizosaccharomyces pombe SMN(GCN4IL) Chimera•Gemin2 complex (12 mg/mL)

Survival motor neuron-like protein 1Survival of motor neuron protein-interacting protein yip11Gcn4p experimental SAS data
Survival motor neuron-like protein 1 Survival of motor neuron protein-interacting protein yip11 Gcn4p Kratky plot
Sample: Survival motor neuron-like protein 1 dimer, 26 kDa Schizosaccharomyces pombe (strain … protein
Survival of motor neuron protein-interacting protein yip11 dimer, 54 kDa Schizosaccharomyces pombe (strain … protein
Gcn4p dimer, 8 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM Na/KPO4 pH 7.0, 150 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at X21, National Synchrotron Light Source (NSLS) on 2011 Oct 21
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 6.6 nm
Dmax 23.3 nm
VolumePorod 320 nm3

SASDL45 – Schizosaccharomyces pombe SMN(GCN4IL) Chimera•Gemin2 complex (6 mg/mL)

Survival motor neuron-like protein 1Survival of motor neuron protein-interacting protein yip11Gcn4p experimental SAS data
Survival motor neuron-like protein 1 Survival of motor neuron protein-interacting protein yip11 Gcn4p Kratky plot
Sample: Survival motor neuron-like protein 1 dimer, 26 kDa Schizosaccharomyces pombe (strain … protein
Survival of motor neuron protein-interacting protein yip11 dimer, 54 kDa Schizosaccharomyces pombe (strain … protein
Gcn4p dimer, 8 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM Na/KPO4 pH 7.0, 150 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at X21, National Synchrotron Light Source (NSLS) on 2011 Oct 21
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 6.6 nm
Dmax 22.9 nm
VolumePorod 325 nm3

SASDH55 – ...RES (SLIVm)

modified stem loop IV poliovirus IRES, nucleotides 278-398 experimental SAS data
modified stem loop IV poliovirus IRES, nucleotides 278-398 Kratky plot
Sample: ...RES, nucleotides 278-398 monomer, 41 kDa Human poliovirus 1 … RNA
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Dec 2
...RES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.5 nm
Dmax 12.0 nm
VolumePorod 94 nm3

SASDL55 – Schizosaccharomyces pombe SMN(GCN4IL) Chimera•Gemin2 complex (4 mg/mL)

Survival motor neuron-like protein 1Survival of motor neuron protein-interacting protein yip11Gcn4p experimental SAS data
Survival motor neuron-like protein 1 Survival of motor neuron protein-interacting protein yip11 Gcn4p Kratky plot
Sample: Survival motor neuron-like protein 1 dimer, 26 kDa Schizosaccharomyces pombe (strain … protein
Survival of motor neuron protein-interacting protein yip11 dimer, 54 kDa Schizosaccharomyces pombe (strain … protein
Gcn4p dimer, 8 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM Na/KPO4 pH 7.0, 150 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at X21, National Synchrotron Light Source (NSLS) on 2011 Oct 21
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 6.4 nm
Dmax 21.9 nm
VolumePorod 315 nm3

SASDH65 – Poly(rC)-binding protein 2 (PCBP2)

Poly(rC)-binding protein 2 experimental SAS data
Poly(rC)-binding protein 2 Kratky plot
Sample: Poly(rC)-binding protein 2 monomer, 40 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jul 16
...RES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.3 nm
Dmax 13.2 nm
VolumePorod 76 nm3

SASDL65 – Schizosaccharomyces pombe SMN(GCN4IL) Chimera•Gemin2 complex (3 mg/mL)

Survival motor neuron-like protein 1Survival of motor neuron protein-interacting protein yip11Gcn4p experimental SAS data
Survival motor neuron-like protein 1 Survival of motor neuron protein-interacting protein yip11 Gcn4p Kratky plot
Sample: Survival motor neuron-like protein 1 dimer, 26 kDa Schizosaccharomyces pombe (strain … protein
Survival of motor neuron protein-interacting protein yip11 dimer, 54 kDa Schizosaccharomyces pombe (strain … protein
Gcn4p dimer, 8 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM Na/KPO4 pH 7.0, 150 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at X21, National Synchrotron Light Source (NSLS) on 2011 Oct 21
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 6.3 nm
Dmax 19.9 nm
VolumePorod 315 nm3

SASDH75 – ...RES (SLIVm) - PCBP2/SLIVm complex

Poly(rC)-binding protein 2modified stem loop IV poliovirus IRES, nucleotides 278-398 experimental SAS data
Poly(rC)-binding protein 2 modified stem loop IV poliovirus IRES, nucleotides 278-398 Kratky plot
Sample: Poly(rC)-binding protein 2 monomer, 40 kDa Homo sapiens protein
...RES, nucleotides 278-398 monomer, 41 kDa Human poliovirus 1 … RNA
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Dec 16
...RES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.7 nm
Dmax 11.5 nm
VolumePorod 162 nm3

SASDL75 – Maltose Binding Protein (MBP) fused to Drosophila Melanogaster SMN186–220: Tetramer analyzed by SVD-EFA SEC-SAXS

Survival motor neuron proteinMaltose/maltodextrin-binding periplasmic protein experimental SAS data
Survival motor neuron protein Maltose/maltodextrin-binding periplasmic protein Kratky plot
Sample: Survival motor neuron protein tetramer, 15 kDa Drosophila melanogaster protein
Maltose/maltodextrin-binding periplasmic protein tetramer, 174 kDa Escherichia coli (strain … protein
Buffer: 20 mM Na/KPO4 pH 7.0, 300 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 19
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 3.9 nm
Dmax 11.3 nm
VolumePorod 340 nm3

SASDH85 – ...RES (SLIVm)

modified stem loop IV poliovirus IRES, nucleotides 278-398Truncated poly(rC)-binding protein 2 (ΔKH3)Truncated poly(rC)-binding protein 2 (ΔKH3) experimental SAS data
modified stem loop IV poliovirus IRES, nucleotides 278-398 Truncated poly(rC)-binding protein 2 (ΔKH3) Truncated poly(rC)-binding protein 2 (ΔKH3) Kratky plot
Sample: ...RES, nucleotides 278-398 monomer, 41 kDa Human poliovirus 1 … RNA
Truncated poly(rC)-binding protein 2 (ΔKH3) monomer, 28 kDa Homo sapiens protein
Truncated poly(rC)-binding protein 2 (ΔKH3) monomer, 28 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jul 1
...RES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.8 nm
Dmax 12.2 nm
VolumePorod 165 nm3

SASDL85 – Maltose Binding Protein (MBP) fused to Drosophila Melanogaster SMN186–220: Octamer analyzed by SVD-EFA SEC-SAXS

Maltose/maltodextrin-binding periplasmic proteinSurvival motor neuron protein experimental SAS data
Maltose/maltodextrin-binding periplasmic protein Survival motor neuron protein Kratky plot
Sample: Maltose/maltodextrin-binding periplasmic protein octamer, 347 kDa Escherichia coli (strain … protein
Survival motor neuron protein octamer, 31 kDa Drosophila melanogaster protein
Buffer: 20 mM Na/KPO4 pH 7.0, 300 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 19
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 5.6 nm
Dmax 17.9 nm
VolumePorod 800 nm3

SASDH95 – Truncated Poly(rC)-binding protein 2 (PCBP2-ΔKH3)

Truncated poly(rC)-binding protein 2 (ΔKH3) experimental SAS data
Truncated poly(rC)-binding protein 2 (ΔKH3) Kratky plot
Sample: Truncated poly(rC)-binding protein 2 (ΔKH3) monomer, 28 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jan 1
...RES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 2.6 nm
Dmax 9.2 nm
VolumePorod 66 nm3

SASDL95 – Drosophila Melanogaster Gemin2-SMN: Octamer analyzed by SVD-EFA SEC-SAXS

Protein Gemin2Survival motor neuron protein experimental SAS data
Protein Gemin2 Survival motor neuron protein Kratky plot
Sample: Protein Gemin2 octamer, 230 kDa Drosophila melanogaster protein
Survival motor neuron protein octamer, 197 kDa Drosophila melanogaster protein
Buffer: 20 mM Na/KPO4 pH 7.0, 300 mM NaCl, 1 mM DTT, pH: 7
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 19
...res an exposed structural motif present in the YG zipper dimer. Nucleic Acids Res 49(13):7644-7664 (2021)
Gupta K, Wen Y, Ninan NS, Raimer AC, Sharp R, Spring AM, Sarachan KL, Johnson MC, Van Duyne GD, Matera AG
RgGuinier 7.8 nm
Dmax 28.7 nm
VolumePorod 2660 nm3

SASDHA5 – ...RES (SLIVm)

modified stem loop IV poliovirus IRES, nucleotides 278-398Truncated poly(rC)-binding protein 2 (ΔKH1-KH2) experimental SAS data
modified stem loop IV poliovirus IRES, nucleotides 278-398 Truncated poly(rC)-binding protein 2 (ΔKH1-KH2) Kratky plot
Sample: ...RES, nucleotides 278-398 monomer, 41 kDa Human poliovirus 1 … RNA
Truncated poly(rC)-binding protein 2 (ΔKH1-KH2) monomer, 18 kDa Homo sapiens protein
Buffer: 5 mM HEPES-KOH, 25 mM KCl, 2 mM MgCl2, 2 mM DTT, 4 % glycerol, 0.1 mM EDTA, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Jul 1
...RES. Nucleic Acids Res (2020)
Beckham SA, Matak MY, Belousoff MJ, Venugopal H, Shah N, Vankadari N, Elmlund H, Nguyen JHC, Semler BL, Wilce MCJ, Wilce JA
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 126 nm3

SASDQF5 – Zinc finger protein 410 (ZNF410 full length)

Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 52 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.6 nm
Dmax 12.3 nm
VolumePorod 108 nm3

SASDAG5 – RNA shaperone Hfq

RNA chaperone Hfq experimental SAS data
DAMMIN model
Sample: RNA chaperone Hfq hexamer, 67 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2008 May 2
Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq. Nucleic Acids Res 39(11):4900-15 (2011)
Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K
RgGuinier 3.2 nm
Dmax 11.2 nm
VolumePorod 110 nm3

SASDQG5 – DNA (Zinc finger protein 410 recognition sequence)

DNA (Zinc finger protein 410 recognition sequence) experimental SAS data
DNA (Zinc finger protein 410 recognition sequence) Kratky plot
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 1.8 nm
Dmax 5.8 nm
VolumePorod 16 nm3

SASDAH5 – Complex of Hfq with DsrA

RNA chaperone HfqRNA DsrA experimental SAS data
SASREF model
Sample: RNA chaperone Hfq hexamer, 67 kDa Escherichia coli protein
RNA DsrA monomer, 12 kDa RNA
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 16
Structural flexibility of RNA as molecular basis for Hfq chaperone function. Nucleic Acids Res 40(16):8072-84 (2012)
Ribeiro Ede A Jr, Beich-Frandsen M, Konarev PV, Shang W, Vecerek B, Kontaxis G, Hämmerle H, Peterlik H, Svergun DI, Bläsi U, Djinović-Carugo K
RgGuinier 4.3 nm
Dmax 14.5 nm
VolumePorod 210 nm3

SASDQH5 – Zinc finger protein 410 (ZNF410 full length) bound to DNA

Zinc finger protein 410DNA (Zinc finger protein 410 recognition sequence) experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 52 kDa Homo sapiens protein
DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 4.4 nm
Dmax 14.3 nm
VolumePorod 76 nm3

SASDQJ5 – Zinc finger protein 410 (ZNF410): N-terminal region with 1-5 zinc fingers

Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 40 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 78 nm3

SASDJK5 – Nucleolysin TIA-1 isoform p40 (TIA-1) bound to TC1 DNA

Nucleolysin TIA-1 isoform p40TC1 experimental SAS data
Nucleolysin TIA-1 isoform p40 TC1 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
TC1 monomer, 3 kDa synthetic construct DNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
...ress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.2 nm
Dmax 15.1 nm
VolumePorod 78 nm3

SASDQK5 – Zinc finger protein 410 (ZNF410): N-terminal region with 1-5 zinc fingers bound to DNA

DNA (Zinc finger protein 410 recognition sequence)Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Zinc finger protein 410 monomer, 40 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2021 Apr 25
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.1 nm
Dmax 14.1 nm
VolumePorod 63 nm3

SASDJL5 – Nucleolysin TIA-1 isoform p40 (TIA-1) bound to UC1 RNA

Nucleolysin TIA-1 isoform p40UC1 experimental SAS data
Nucleolysin TIA-1 isoform p40 UC1 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
UC1 monomer, 3 kDa synthetic construct RNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Jun 26
...ress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.3 nm
Dmax 14.4 nm
VolumePorod 77 nm3

SASDQL5 – Zinc finger protein 410 (ZNF410): C-terminal region with 1-5 zinc fingers

Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: Zinc finger protein 410 monomer, 29 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.0 nm
Dmax 9.6 nm
VolumePorod 58 nm3

SASDJM5 – Modified nucleolysin TIA-1 isoform p40 (TIA-1 APO)

Modified Nucleolysin TIA-1 isofrom p40 experimental SAS data
Modified Nucleolysin TIA-1 isofrom p40 Kratky plot
Sample: Modified Nucleolysin TIA-1 isofrom p40 monomer, 42 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 60 mM KCl, 0.5 M arginine-HCl, 1 mM MgCl2, 2 mM DTT, 0.5 mM EDTA, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2020 Jul 7
...ress granule marker protein TIA-1. Nucleic Acids Res (2021)
Loughlin FE, West DL, Gunzburg MJ, Waris S, Crawford SA, Wilce MCJ, Wilce JA
RgGuinier 3.2 nm
Dmax 12.7 nm
VolumePorod 62 nm3

SASDQM5 – Zinc finger protein 410 (ZNF410): C-terminal region with 1-5 zinc fingers bound to DNA

DNA (Zinc finger protein 410 recognition sequence)Zinc finger protein 410 experimental SAS data
BILBOMD model
Sample: DNA (Zinc finger protein 410 recognition sequence) monomer, 11 kDa DNA
Zinc finger protein 410 monomer, 29 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, 0.1% v/v β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Sep 30
Allosteric autoregulation of DNA binding via a DNA-mimicking protein domain: a biophysical study of ZNF410-DNA interaction using small angle X-ray scattering. Nucleic Acids Res (2023)
Kaur G, Ren R, Hammel M, Horton JR, Yang J, Cao Y, He C, Lan F, Lan X, Blobel GA, Blumenthal RM, Zhang X, Cheng X
RgGuinier 3.1 nm
Dmax 11.9 nm
VolumePorod 52 nm3

SASDGP5 – Vibrio cholerae DciA

DciA experimental SAS data
DciA Kratky plot
Sample: DciA monomer, 18 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Mar 26
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. Nucleic Acids Res (2021)
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Che...
RgGuinier 2.7 nm
Dmax 10.1 nm
VolumePorod 26 nm3

SASDGQ5 – Vibrio cholerae hexameric DnaB helicase with bound ATP (VcDnaB.ATP)

Replicative DNA helicase (DnaB) experimental SAS data
Replicative DNA helicase (DnaB) Kratky plot
Sample: Replicative DNA helicase (DnaB) hexamer, 317 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 1 mM ATP, pH: 8.8
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Oct 4
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. Nucleic Acids Res (2021)
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Che...
RgGuinier 4.6 nm
Dmax 13.0 nm
VolumePorod 585 nm3

SASDGR5 – ...resence of bound ATP (VcDnaB.DciA.ATP)

DnaB helicase complexed with ATPDciA experimental SAS data
DnaB helicase complexed with ATP DciA Kratky plot
Sample: DnaB helicase complexed with ATP hexamer, 317 kDa Vibrio cholerae serotype … protein
DciA , 55 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 1 mM ATP, pH: 8.8
Experiment: SAXS data collected at SWING, SOLEIL on 2018 Oct 4
Study of the DnaB:DciA interplay reveals insights into the primary mode of loading of the bacterial replicative helicase. Nucleic Acids Res (2021)
Marsin S, Adam Y, Cargemel C, Andreani J, Baconnais S, Legrand P, Li de la Sierra-Gallay I, Humbert A, Aumont-Nicaise M, Velours C, Ochsenbein F, Durand D, Le Cam E, Walbott H, Possoz C, Quevillon-Che...
RgGuinier 5.0 nm
Dmax 15.6 nm
VolumePorod 670 nm3

SASDMR5 – Tn3 family transposase (TnpA WT)

TnpA transposase experimental SAS data
GASBOR model
Sample: TnpA transposase dimer, 234 kDa Bacillus thuringiensis serovar … protein
Buffer: 50 mM HEPES, 200 mM NaCl, 100 mM L-Arg HCL, pH: 7.9
Experiment: SAXS data collected at SWING, SOLEIL on 2017 Nov 2
AFM-based force spectroscopy unravels stepwise formation of the DNA transposition complex in the widespread Tn3 family mobile genetic elements. Nucleic Acids Res (2023)
Fernandez M, Shkumatov AV, Liu Y, Stulemeijer C, Derclaye S, Efremov RG, Hallet B, Alsteens D
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 480 nm3

SASDGS5 – MvaT (low salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 50 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.6 nm
Dmax 14.7 nm
VolumePorod 47 nm3

SASDDT5 – Ribonucleoprotein complex of nonstructural protein sigma NS bound to 20mer RNA (NS-RNP20)

Nonstructural protein sigma NS20mer RNA (unstructured) experimental SAS data
Nonstructural protein sigma NS 20mer RNA (unstructured) Kratky plot
Sample: Nonstructural protein sigma NS octamer, 325 kDa Avian orthoreovirus protein
20mer RNA (unstructured) dimer, 13 kDa RNA
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Feb 25
Stability of local secondary structure determines selectivity of viral RNA chaperones. Nucleic Acids Res (2018)
...rese AN, Mojzes P, Cockburn JJB, Lamb DC, Tuma R
RgGuinier 7.8 nm
Dmax 38.0 nm
VolumePorod 964 nm3

SASDGT5 – MvaT (high salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 300 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.8 nm
Dmax 15.8 nm
VolumePorod 50 nm3

SASDQT5 – NPL3 protein RNA recognition motifs 1 and 2 (RRM1,2) wild-type

Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 experimental SAS data
Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 Kratky plot
Sample: Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 monomer, 18 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM NaPO4, 50 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2020 Feb 20
Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA. Nucleic Acids Res (2022)
Keil P, Wulf A, Kachariya N, Reuscher S, Hühn K, Silbern I, Altmüller J, Keller M, Stehle R, Zarnack K, Sattler M, Urlaub H, Sträßer K
RgGuinier 2.0 nm
Dmax 6.8 nm
VolumePorod 24 nm3

SASDDU5 – Nonstructural protein sigma NS - apoprotein

Nonstructural protein sigma NS experimental SAS data
Nonstructural protein sigma NS Kratky plot
Sample: Nonstructural protein sigma NS hexamer, 244 kDa Avian orthoreovirus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Feb 25
Stability of local secondary structure determines selectivity of viral RNA chaperones. Nucleic Acids Res (2018)
...rese AN, Mojzes P, Cockburn JJB, Lamb DC, Tuma R
RgGuinier 5.5 nm
Dmax 23.1 nm
VolumePorod 670 nm3

SASDQU5 – NPL3 protein RNA recognition motifs 1 and 2 (RRM1,2) P196D/A197D linker mutant

Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 experimental SAS data
Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 Kratky plot
Sample: Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 monomer, 18 kDa Saccharomyces cerevisiae (strain … protein
Buffer: 20 mM NaPO4, 50 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2020 Feb 20
Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA. Nucleic Acids Res (2022)
Keil P, Wulf A, Kachariya N, Reuscher S, Hühn K, Silbern I, Altmüller J, Keller M, Stehle R, Zarnack K, Sattler M, Urlaub H, Sträßer K
RgGuinier 1.9 nm
Dmax 6.7 nm
VolumePorod 25 nm3