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26 hits found for Tsai

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)
...Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 5.4 nm
Dmax 19.5 nm
VolumePorod 170 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)
...Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.3 nm
Dmax 26.9 nm
VolumePorod 330 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)
...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)
...Tsai MS, Ellenberger T, Pascal JM, Kim IK, Tainer JA, Tomkinson AE
RgGuinier 6.2 nm
Dmax 27.9 nm
VolumePorod 675 nm3

SASDPZ3 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 3’ss-ds DNA junction NER substrate

DNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunitReplication protein A 14 kDa subunit3-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
3-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
...Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.3 nm
Dmax 14.7 nm
VolumePorod 189 nm3

SASDP24 – Complex of XPA1-239 and RPAΔ32NΔ70N complex engaged on 5’ss-ds DNA junction NER substrate

Replication protein A 14 kDa subunitDNA repair protein complementing XP-A cellsReplication protein A 70 kDa DNA-binding subunitReplication protein A 32 kDa subunit5-prime ss-ds DNA junction NER model substrate experimental SAS data
MES-FOXS model
Sample: Replication protein A 14 kDa subunit monomer, 14 kDa Homo sapiens protein
DNA repair protein complementing XP-A cells monomer, 27 kDa Homo sapiens protein
Replication protein A 70 kDa DNA-binding subunit monomer, 49 kDa Homo sapiens protein
Replication protein A 32 kDa subunit monomer, 25 kDa Homo sapiens protein
5-prime ss-ds DNA junction NER model substrate monomer, 17 kDa DNA
Buffer: 20 mM Tris pH 8.0, 150 mM NaCl, 2% glycerol, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Mar 4
Two interaction surfaces between XPA and RPA organize the preincision complex in nucleotide excision repair Proceedings of the National Academy of Sciences 119(34) (2022)
...Tsai C, Tsai M, Kee M, Tainer J, Yeo J, Chazin W, Schärer O
RgGuinier 4.6 nm
Dmax 16.5 nm
VolumePorod 220 nm3

SASDT35 – N-cadherin extracellular domains EC1-EC5

Cadherin-2 experimental SAS data
Cadherin-2 Kratky plot
Sample: Cadherin-2 dimer, 123 kDa Mus musculus protein
Buffer: 10 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 8
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 1
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell 187(5):1296-1311.e26 (2024)
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
RgGuinier 8.8 nm
Dmax 40.0 nm
VolumePorod 496 nm3

SASDT45 – N-cadherin extracellular domains EC4-EC5

Cadherin-2 experimental SAS data
Cadherin-2 Kratky plot
Sample: Cadherin-2 monomer, 24 kDa Mus musculus protein
Buffer: 10 mM HEPES, 150 mM NaCl, 3 mM CaCl2, 0.02% NaN3, pH: 8
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 1
Rapid simulation of glycoprotein structures by grafting and steric exclusion of glycan conformer libraries. Cell 187(5):1296-1311.e26 (2024)
Tsai YX, Chang NE, Reuter K, Chang HT, Yang TJ, von Bülow S, Sehrawat V, Zerrouki N, Tuffery M, Gecht M, Grothaus IL, Colombi Ciacchi L, Wang YS, Hsu MF, Khoo KH, Hummer G, Hsu SD, Hanus C, Sikora M
RgGuinier 3.4 nm
Dmax 12.6 nm
VolumePorod 63 nm3

SASDVL5 – Small EDRK-rich factor 1 (SERF1a)

Isoform Short of Small EDRK-rich factor 1 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Mar 11
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.4 nm
Dmax 8.0 nm
VolumePorod 9 nm3

SASDVM5 – HTT-3 peptide

HTT3 experimental SAS data
ROSETTA model
Sample: HTT3 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 May 20
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.0 nm

SASDVN5 – NT17 peptide

NT17 experimental SAS data
ROSETTA model
Sample: NT17 monomer, 2 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Oct 21
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 1.2 nm
Dmax 4.0 nm
VolumePorod 5 nm3

SASDVP5 – HTT0 peptide

HTT0 experimental SAS data
ROSETTA model
Sample: HTT0 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2023 Nov 10
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 1.5 nm
Dmax 6.0 nm
VolumePorod 4 nm3

SASDVQ5 – HTT1 peptide

HTT1 experimental SAS data
HTT1 Kratky plot
Sample: HTT1 dimer, 8 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Feb 3
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 1.9 nm
Dmax 7.0 nm
VolumePorod 18 nm3

SASDVR5 – Small EDRK-rich factor 1 (SERF1a) bound to NT17 peptide

Isoform Short of Small EDRK-rich factor 1NT17 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
NT17 dimer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 Oct 21
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm

SASDVS5 – Small EDRK-rich factor 1 (SERF1a) bound to HTT-3 peptide

Isoform Short of Small EDRK-rich factor 1HTT3 experimental SAS data
ROSETTA model
Sample: Isoform Short of Small EDRK-rich factor 1 monomer, 7 kDa Homo sapiens protein
HTT3 monomer, 4 kDa synthetic construct protein
Buffer: Sodium phosphate buffer, pH: 7.4
Experiment: SAXS data collected at TPS13A, NSRRC on 2021 May 20
Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation. IUCrJ (2024)
...Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US
RgGuinier 2.3 nm
Dmax 7.2 nm
VolumePorod 9 nm3

SASDJN2 – Tyrosyl-DNA phosphodiesterase 1 (TDP1)

Tyrosyl-DNA phosphodiesterase 1 experimental SAS data
BILBOMD model
Sample: Tyrosyl-DNA phosphodiesterase 1 monomer, 71 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 26
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
...Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 3.2 nm
Dmax 11.7 nm
VolumePorod 143 nm3

SASDM47 – NAD glycohydrolase (NADase)

NAD glycohydrolase experimental SAS data
BILBOMD model
Sample: NAD glycohydrolase monomer, 47 kDa Streptococcus pyogenes M1 … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 16
Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection. Commun Biol 6(1):124 (2023)
Tsai WJ, Lai YH, Shi YA, Hammel M, Duff AP, Whitten AE, Wilde KL, Wu CM, Knott R, Jeng US, Kang CY, Hsu CY, Wu JL, Tsai PJ, Chiang-Ni C, Wu JJ, Lin YS, Liu CC, Senda T, Wang S
RgGuinier 3.0 nm
Dmax 103.0 nm
VolumePorod 66 nm3

SASDEU7 – Stator protein FlaG soluble domain

Conserved flagellar protein FlaG soluble domain experimental SAS data
Conserved flagellar protein FlaG soluble domain Kratky plot
Sample: Conserved flagellar protein FlaG soluble domain monomer, 15 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.7 nm
Dmax 18.0 nm
VolumePorod 133 nm3

SASDJQ2 – Dephosphorylated tyrosyl-DNA phosphodiesterase 1 (TDP1-Ppi)

Tyrosyl-DNA phosphodiesterase 1 (dephosphorylated) experimental SAS data
BILBOMD model
Sample: Tyrosyl-DNA phosphodiesterase 1 (dephosphorylated) monomer, 71 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 26
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
...Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 3.2 nm
Dmax 16.5 nm
VolumePorod 141 nm3

SASDM57 – NAD glycohydrolase (NADase)/Streptolysin O (SLO) complex (SAXS with additional contrast variation SANS data)

NAD glycohydrolaseStreptolysin O (T66M) experimental SAS data
BILBOMD model
Sample: NAD glycohydrolase monomer, 47 kDa Streptococcus pyogenes M1 … protein
Streptolysin O (T66M) monomer, 63 kDa Streptococcus pyogenes serotype … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 16
Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection. Commun Biol 6(1):124 (2023)
Tsai WJ, Lai YH, Shi YA, Hammel M, Duff AP, Whitten AE, Wilde KL, Wu CM, Knott R, Jeng US, Kang CY, Hsu CY, Wu JL, Tsai PJ, Chiang-Ni C, Wu JJ, Lin YS, Liu CC, Senda T, Wang S
RgGuinier 4.8 nm
Dmax 18.4 nm
VolumePorod 125 nm3

SASDES7 – Stator protein complex FlaG/FlaF

Conserved flagellar protein FStator protein FlaG soluble domain experimental SAS data
MULTIFOXS model
Sample: Conserved flagellar protein F dimer, 32 kDa Sulfolobus acidocaldarius protein
Stator protein FlaG soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 109 nm3

SASDJP2 – Truncated tyrosyl-DNA phosphodiesterase 1 (TDP1 149-608)

Tyrosyl-DNA phosphodiesterase 1 (149-608) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Tyrosyl-DNA phosphodiesterase 1 (149-608) monomer, 53 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 Sep 18
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
...Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 2.3 nm
Dmax 7.0 nm
VolumePorod 80 nm3

SASDEV7 – Stator protein complex FlaG/FlaF-I96Y

Stator protein FlaG soluble domainConserved flagellar protein FlaF-I96Y soluble domain experimental SAS data
BILBOMD model
Sample: Stator protein FlaG soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Conserved flagellar protein FlaF-I96Y soluble domain dimer, 33 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 2.7 nm
Dmax 8.2 nm
VolumePorod 90 nm3

SASDJS2 – Truncated DNA ligase 3 bound to tyrosyl-DNA phosphodiesterase 1 (LigIIIα(170-755)/TDP1 complex)

Tyrosyl-DNA phosphodiesterase 1Isoform 3 of DNA ligase 3 (DNA ligase III alpha) experimental SAS data
BILBOMD model
Sample: Tyrosyl-DNA phosphodiesterase 1 monomer, 71 kDa Homo sapiens protein
Isoform 3 of DNA ligase 3 (DNA ligase III alpha) monomer, 68 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 40 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jul 5
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
...Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 4.5 nm
Dmax 18.0 nm
VolumePorod 211 nm3

SASDET7 – Stator protein complex FlaG-V118K/FlaF

Conserved flagellar protein FStator protein FlaG-V118K soluble domain experimental SAS data
MULTIFOXS model
Sample: Conserved flagellar protein F dimer, 32 kDa Sulfolobus acidocaldarius protein
Stator protein FlaG-V118K soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 108 nm3

SASDJR2 – DNA ligase 3 bound to tyrosyl-DNA phosphodiesterase 1 (LigIIIα/TDP1 complex)

DNA ligase 3 (DNA ligase III alpha)Tyrosyl-DNA phosphodiesterase 1 experimental SAS data
BILBOMD model
Sample: DNA ligase 3 (DNA ligase III alpha) , Homo sapiens protein
Tyrosyl-DNA phosphodiesterase 1 monomer, 71 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 40 mM HEPES, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 10
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
...Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 6.5 nm
Dmax 25.5 nm
VolumePorod 790 nm3