Browse by ORGANISM: other species

SASDEG6 – Epstein-Barr nuclear antigen 2 (EBNA2 Type2, amino acids 348-422)

Epstein-Barr nuclear antigen 2 experimental SAS data
DAMMIN model
Sample: Epstein-Barr nuclear antigen 2 dimer, 16 kDa Human gammaherpesvirus 4 protein
Buffer: 20mM Tris-HCl, 100mM NaCl, 2% Sucrose and 1mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Sep 23
Increased association between Epstein-Barr virus EBNA2 from type 2 strains and the transcriptional repressor BS69 restricts B cell growth (2018)
Ponnusamy R, Khatri R, Correia P, Mancini E, Farrell P, West M
RgGuinier 2.8 nm
Dmax 10.4 nm
VolumePorod 20 nm3

SASDDH3 – Solution Structure of Archaeal Biofilm Regulator 2 (AbfR2)

Transcriptional regulator Lrs14-like protein experimental SAS data
DAMMIF model
Sample: Transcriptional regulator Lrs14-like protein dimer, 33 kDa Sulfolobus acidocaldarius protein
Buffer: 300 mM NaCl, 20 mM HEPES, pH 7.5, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 May 5
Crystal structure of an Lrs14-like archaeal biofilm regulator from Sulfolobus acidocaldarius. Acta Crystallogr D Struct Biol 74(Pt 11):1105-1114 (2018)
Vogt MS, Völpel SL, Albers SV, Essen LO, Banerjee A
RgGuinier 2.9 nm
Dmax 10.0 nm
VolumePorod 57 nm3

SASDDY5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the resting state (apo), in stealth DDM detergents

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.0 nm
Dmax 17.9 nm
VolumePorod 396 nm3

SASDDZ5 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 7.5

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.3 nm
Dmax 18.4 nm
VolumePorod 407 nm3

SASDD26 – AMPA subtype ionotropic Glutamate receptor GluA2 in the AMPA bound state, in stealth DDM detergents, pH 5.5

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 10 mM AMPA, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 5.5
Experiment: SANS data collected at KWS1, FRM2 on 2017 Sep 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.5 nm
Dmax 18.9 nm
VolumePorod 899 nm3

SASDD36 – AMPA subtype ionotropic Glutamate receptor GluA2 in the GYKI-53655 bound state, in stealth DDM detergents

Glutamate receptor 2 experimental SAS data
Sample: Glutamate receptor 2 monomer, 368 kDa Rattus norvegicus protein
Buffer: D2O based buffer. 1 mM GYKI-53655, 20 mM Tris/DCl, 100 mM NaCl, 0.5 mM deuterated n-dodecyl-β-D-maltopyranoside (synthesized to match out at 100% D2O), pH: 7.5
Experiment: SANS data collected at KWS1, FRM2 on 2016 Oct 19
Small-angle neutron scattering studies on the AMPA receptor GluA2 in the resting, AMPA-bound and GYKI-53655-bound states. IUCrJ 5(Pt 6):780-793 (2018)
Larsen AH, Dorosz J, Thorsen TS, Johansen NT, Darwish T, Midtgaard SR, Arleth L, Kastrup JS
RgGuinier 6.3 nm
Dmax 18.6 nm
VolumePorod 384 nm3

SASDEF3 – Paenibacillus xanthan lyase (PXL) at 4 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chem Biol 26(2):191-202.e6 (2019)
Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen JN, Rasmussen KK, Agarwal S, Sainathan RK, Monrad RN, Svendsen A, Nielsen JE, Lo Leggio L, Rand KD
RgGuinier 3.7 nm
Dmax 13.1 nm
VolumePorod 137 nm3

SASDEG3 – Paenibacillus xanthan lyase (PXL) at 20 °C

Paenibacillus xanthan lyase experimental SAS data
Paenibacillus xanthan lyase Kratky plot
Sample: Paenibacillus xanthan lyase monomer, 113 kDa Paenibacillus sp-62047 protein
Buffer: 20 mM Tris,, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 15
Structure and Dynamics of a Promiscuous Xanthan Lyase from Paenibacillus nanensis and the Design of Variants with Increased Stability and Activity. Cell Chem Biol 26(2):191-202.e6 (2019)
Jensen PF, Kadziola A, Comamala G, Segura DR, Anderson L, Poulsen JN, Rasmussen KK, Agarwal S, Sainathan RK, Monrad RN, Svendsen A, Nielsen JE, Lo Leggio L, Rand KD
RgGuinier 3.8 nm
Dmax 13.8 nm
VolumePorod 134 nm3

SASDD45 – Type II toxin-antitoxin system HicB family antitoxin - HicB protein

Type II toxin-antitoxin system HicB family antitoxin experimental SAS data
PYMOL model
Sample: Type II toxin-antitoxin system HicB family antitoxin tetramer, 63 kDa Burkholderia pseudomallei protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 28
The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA. J Biol Chem (2018)
Winter AJ, Williams C, Isupov MN, Crocker H, Gromova M, Marsh P, Wilkinson OJ, Dillingham MS, Harmer NJ, Titball RW, Crump MP
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 112 nm3

SASDD55 – Type II toxin-antitoxin system HicB family antitoxin - HicB protein - bound to addiction module toxin, HicA

Type II toxin-antitoxin system HicB family antitoxinAddiction module toxin, HicA experimental SAS data
PYMOL model
Sample: Type II toxin-antitoxin system HicB family antitoxin tetramer, 63 kDa Burkholderia pseudomallei protein
Addiction module toxin, HicA monomer, 7 kDa Burkholderia pseudomallei protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 27
The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA. J Biol Chem (2018)
Winter AJ, Williams C, Isupov MN, Crocker H, Gromova M, Marsh P, Wilkinson OJ, Dillingham MS, Harmer NJ, Titball RW, Crump MP
RgGuinier 3.2 nm
Dmax 11.0 nm
VolumePorod 110 nm3