Browse by ORGANISM: other species

SASDBZ8 – Single stranded poly-deoxyadenosine DNA (30mer, dA30) in 100 mM NaCl

Poly-deoxyadenosine (30mer) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Poly-deoxyadenosine (30mer) monomer, 9 kDa DNA
Buffer: 1mM Na MOPS, 100mM NaCl, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Apr 1
The impact of base stacking on the conformations and electrostatics of single-stranded DNA. Nucleic Acids Res 45(7):3932-3943 (2017)
Plumridge A, Meisburger SP, Andresen K, Pollack L
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 16 nm3

SASDB29 – Single stranded poly-deoxyadenosine DNA (30mer, dA30) in 200 mM NaCl

Poly-deoxyadenosine (30mer) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Poly-deoxyadenosine (30mer) monomer, 9 kDa DNA
Buffer: 1mM Na MOPS, 200mM NaCl, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Apr 1
The impact of base stacking on the conformations and electrostatics of single-stranded DNA. Nucleic Acids Res 45(7):3932-3943 (2017)
Plumridge A, Meisburger SP, Andresen K, Pollack L
RgGuinier 2.7 nm
Dmax 9.5 nm
VolumePorod 15 nm3

SASDB39 – Single stranded poly-deoxythymidine DNA (30mer, dT30) in 100 mM NaCl

Poly-deoxythymidine (30mer) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Poly-deoxythymidine (30mer) monomer, 9 kDa DNA
Buffer: 1mM Na MOPS, 100mM NaCl, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Apr 1
The impact of base stacking on the conformations and electrostatics of single-stranded DNA. Nucleic Acids Res 45(7):3932-3943 (2017)
Plumridge A, Meisburger SP, Andresen K, Pollack L
RgGuinier 2.8 nm

SASDB49 – Single stranded poly-deoxythymidine DNA (30mer, dT30) in 200 mM NaCl

Poly-deoxythymidine (30mer) experimental SAS data
CUSTOM IN-HOUSE model
Sample: Poly-deoxythymidine (30mer) monomer, 9 kDa DNA
Buffer: 1mM Na MOPS, 200mM NaCl, pH: 7
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Apr 1
The impact of base stacking on the conformations and electrostatics of single-stranded DNA. Nucleic Acids Res 45(7):3932-3943 (2017)
Plumridge A, Meisburger SP, Andresen K, Pollack L
RgGuinier 2.7 nm

SASDBE7 – ESX-5 type VII secretion system protein EccC5

ESX-5 type VII secretion system protein EccC5 experimental SAS data
ESX-5 type VII secretion system protein EccC5 Rg histogram
Sample: ESX-5 type VII secretion system protein EccC5 monomer, 142 kDa Mycobacterium xenopi RIVM700367 protein
Buffer: 20 mM Tris 200 mM NaCl 5%(v/v) Glycerol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jul 15
Structure of the mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis. Nat Microbiol 2:17047 (2017)
Beckham KS, Ciccarelli L, Bunduc CM, Mertens HD, Ummels R, Lugmayr W, Mayr J, Rettel M, Savitski MM, Svergun DI, Bitter W, Wilmanns M, Marlovits TC, Parret AH, Houben EN
RgGuinier 6.2 nm
Dmax 23.0 nm
VolumePorod 255 nm3

SASDJB2 – Restriction endonuclease R.AgeI in apo form, monomeric

Type-2 restriction enzyme AgeI experimental SAS data
DAMMIN model
Sample: Type-2 restriction enzyme AgeI monomer, 31 kDa Thalassobius gelatinovorus protein
Buffer: 10 mM Tris-HCl, pH 7.5, 150 mM NaCl, 5 mM CaClâ‚‚, 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

SASDJC2 – Restriction 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: Type-2 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 CaClâ‚‚, 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

SASDBD3 – Leishmania braziliensis heat shock protein 90 (Hsp90).

Leishmania braziliensis heat shock protein 90 (Hsp90) experimental SAS data
DAMMIN model
Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) dimer, 166 kDa Leishmania braziliensis protein
Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1
Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC
RgGuinier 5.3 nm
Dmax 21.0 nm
VolumePorod 380 nm3

SASDBE3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N domain.

Leishmania braziliensis heat shock protein 90 (Hsp90) N domain experimental SAS data
DAMMIN model
Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) N domain monomer, 26 kDa Leishmania braziliensis protein
Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1
Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC
RgGuinier 2.0 nm
Dmax 7.5 nm
VolumePorod 40 nm3

SASDBF3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains.

Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains experimental SAS data
DAMMIN model
Sample: Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains monomer, 62 kDa Leishmania braziliensis protein
Buffer: 25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1
Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC
RgGuinier 3.2 nm
Dmax 13.0 nm
VolumePorod 89 nm3