SASDBV6 – GppNHp bound form of C-terminal deletion mutant of ObgE from E.coli (ObgE_340 with GppNHp)

GTPase ObgE/CgtA experimental SAS data
DAMMIN model
Sample: GTPase ObgE/CgtA monomer, 39 kDa Escherichia coli protein
Buffer: 20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 µM GppNHp, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Mar 12
Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence. J Biol Chem 292(14):5871-5883 (2017)
Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W
RgGuinier 3.1 nm
Dmax 11.4 nm
VolumePorod 72 nm3

SASDBA9 – E. coli CcdB2-CcdA2-CcdB2 toxin/antitoxin heterohexamer complex

Toxin CcdBAntitoxin CcdAToxin CcdB experimental SAS data
MODELLER model
Sample: Toxin CcdB dimer, 23 kDa Escherichia coli protein
Antitoxin CcdA dimer, 17 kDa Escherichia coli protein
Toxin CcdB dimer, 23 kDa Escherichia coli protein
Buffer: 10 mM Tris 50 mM NaCl, pH: 7.3
Experiment: SAXS data collected at SWING, SOLEIL on 2013 Jul 24
Molecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon. Nucleic Acids Res 45(6):2937-2950 (2017)
Vandervelde A, Drobnak I, Hadži S, Sterckx YG, Welte T, De Greve H, Charlier D, Efremov R, Loris R, Lah J
RgGuinier 3.4 nm
Dmax 12.0 nm
VolumePorod 92 nm3

SASDBB9 – GDP bound form of full length ObgE from E.coli (ObgE_FL with GDP)

GTPase ObgE/CgtA experimental SAS data
DAMMIN model
Sample: GTPase ObgE/CgtA monomer, 44 kDa Escherichia coli protein
Buffer: 20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 uM GDP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Jun 17
Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence. J Biol Chem 292(14):5871-5883 (2017)
Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W
RgGuinier 3.5 nm
Dmax 16.0 nm
VolumePorod 94673 nm3

SASDBC9 – GDP bound form of C-terminal deletion mutant of ObgE from E.coli (ObgE_340 with GDP)

GTPase ObgE/CgtA experimental SAS data
DAMMIN model
Sample: GTPase ObgE/CgtA monomer, 39 kDa Escherichia coli protein
Buffer: 20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 uM GDP, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-2000, on 2015 Feb 1
Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence. J Biol Chem 292(14):5871-5883 (2017)
Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W
RgGuinier 3.0 nm
Dmax 11.0 nm
VolumePorod 70673 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 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

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 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

SASDB99 – Extracellular assembly of the human TSLP:TSLPR:IL-7Ralpha complex

Thymic stromal lymphopoietinInterleukin-7 receptor subunit alphaCytokine receptor-like factor 2 experimental SAS data
ALLOSMOD model
Sample: Thymic stromal lymphopoietin monomer, 15 kDa Homo sapiens protein
Interleukin-7 receptor subunit alpha monomer, 26 kDa Homo sapiens protein
Cytokine receptor-like factor 2 monomer, 24 kDa Homo sapiens protein
Buffer: 10 mM Hepes, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Apr 8
Structure and antagonism of the receptor complex mediated by human TSLP in allergy and asthma. Nat Commun 8:14937 (2017)
Verstraete K, Peelman F, Braun H, Lopez J, Van Rompaey D, Dansercoer A, Vandenberghe I, Pauwels K, Tavernier J, Lambrecht BN, Hammad H, De Winter H, Beyaert R, Lippens G, Savvides SN
RgGuinier 3.1 nm
Dmax 10.3 nm
VolumePorod 98 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

4779 hits found.