Browse by DISSEMINATION: Published

SASDNV6 – Early E1A protein, SEC-SAXS data

Early E1A protein experimental SAS data
Early E1A protein Kratky plot
Sample: Early E1A protein monomer, 13 kDa Human adenovirus C … protein
Buffer: 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH: 7
Experiment: SAXS data collected at SWING, SOLEIL on 2019 Mar 24
Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nat Struct Mol Biol (2022)
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB
RgGuinier 3.6 nm
Dmax 17.5 nm
VolumePorod 45 nm3

SASDNX3 – Calcium-bound Calmodulin, including structural models

Calmodulin-1 experimental SAS data
Calcium-bound Calmodulin, including structural models Rg histogram
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 33 nm3

SASDNY3 – Calcium-bound Calmodulin complexed with Calmidazolium

Calmodulin-1Calmidazolium experimental SAS data
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Calmidazolium monomer, 1 kDa
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 1.7 nm
Dmax 5.2 nm
VolumePorod 30 nm3

SASDNT5 – Bradyzoite Pseudokinase 1 (amino acids 61-377)

Rhoptry kinase family protein experimental SAS data
Sample: Rhoptry kinase family protein tetramer, 143 kDa Toxoplasma gondii (strain … protein
Buffer: 20 mM HEPES, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2016 Apr 19
Divergent kinase WNG1 is regulated by phosphorylation of an atypical activation sub-domain. Biochem J (2022)
Dewangan PS, Beraki TG, Paiz EA, Appiah Mensah D, Chen Z, Reese ML
RgGuinier 3.8 nm
Dmax 11.5 nm
VolumePorod 207 nm3

SASDHB5 – RelA Homology Domain of p50/RelA heterodimer

NF-kappa-B p105 subunit 39-350Transcription factor p65 19-321 experimental SAS data
MULTIFOXS model
Sample: NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Transcription factor p65 19-321 monomer, 35 kDa Mus musculus protein
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 110 nm3

SASDHC5 – Nuclear factor kB p50/RelA heterodimer

Transcription factor p65 19-549NF-kappa-B p105 subunit 39-350 experimental SAS data
BILBOMD model
Sample: Transcription factor p65 19-549 monomer, 58 kDa Mus musculus protein
NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 4.6 nm
Dmax 15.3 nm
VolumePorod 183 nm3

SASDHD5 – Transactivation domain of RelA

Transcription factor p65 340-549 experimental SAS data
MULTIFOXS model
Sample: Transcription factor p65 340-549 monomer, 23 kDa Mus musculus protein
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 2.7 nm
Dmax 8.2 nm
VolumePorod 59 nm3

SASDHE5 – Rel Homology Domain of p50/RelA bound to IFN kB site DNA

NF-kappa-B p105 subunit 39-350Transcription factor p65 19-321IFN kB DNA experimental SAS data
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 IFN kB DNA Kratky plot
Sample: NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Transcription factor p65 19-321 monomer, 35 kDa Mus musculus protein
IFN kB DNA monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 4.3 nm
Dmax 13.0 nm
VolumePorod 237 nm3

SASDHF5 – Rel Homology Domain of p50/RelA bound to Urokinase kB site DNA

NF-kappa-B p105 subunit 39-350Transcription factor p65 19-321Urokinase kB experimental SAS data
NF-kappa-B p105 subunit 39-350 Transcription factor p65 19-321 Urokinase kB Kratky plot
Sample: NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
Transcription factor p65 19-321 monomer, 35 kDa Mus musculus protein
Urokinase kB monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Jun 11
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 4.1 nm
Dmax 13.0 nm
VolumePorod 244 nm3

SASDHG5 – Nuclear factor kB p50/RelA bound to IFN kB site DNA

Transcription factor p65 19-549NF-kappa-B p105 subunit 39-350IFN kB DNA experimental SAS data
Transcription factor p65 19-549 NF-kappa-B p105 subunit 39-350 IFN kB DNA Kratky plot
Sample: Transcription factor p65 19-549 monomer, 58 kDa Mus musculus protein
NF-kappa-B p105 subunit 39-350 monomer, 36 kDa Mus musculus protein
IFN kB DNA monomer, 8 kDa DNA
Buffer: 25 mM Tris.Cl, 150 mM NaCl, 1 mM DTT, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 4
An intrinsically disordered transcription activation domain increases the DNA binding affinity and reduces the specificity of NFκB p50/RelA. J Biol Chem :102349 (2022)
Baughman HER, Narang D, Chen W, Villagrán Suárez AC, Lee J, Bachochin MJ, Gunther TR, Wolynes PG, Komives EA
RgGuinier 5.1 nm
Dmax 18.9 nm
VolumePorod 314 nm3