SASDMZ4 – Mixture of estrogen-related receptor gamma:Inverse repeat IR3 DNA - 6:3 and 2:1 complexes - at 2.9 mg/ml

Estrogen-related receptor gammaInverse repeat IR3 DNA experimental SAS data
SASREF MX model
Sample: Estrogen-related receptor gamma hexamer, 230 kDa Homo sapiens protein
Inverse repeat IR3 DNA trimer, 46 kDa DNA
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 100 mM KCl, 5 mM MgCl2, 1% (v/v) glycerol, and 1 mM CHAPS, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 3
Reconstruction of Quaternary Structure from X-ray Scattering by Equilibrium Mixtures of Biological Macromolecules Biochemistry 52(39):6844-6855 (2013)
Petoukhov M, Billas I, Takacs M, Graewert M, Moras D, Svergun D
RgGuinier 4.7 nm
Dmax 14.6 nm

SASDM25 – Mixture of estrogen-related receptor gamma:Inverse repeat IR3 DNA - 6:3 and 2:1 complexes - at 1.9 mg/ml

Estrogen-related receptor gammaInverse repeat IR3 DNA experimental SAS data
SASREF MX model
Sample: Estrogen-related receptor gamma hexamer, 230 kDa Homo sapiens protein
Inverse repeat IR3 DNA trimer, 46 kDa DNA
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 100 mM KCl, 5 mM MgCl2, 1% (v/v) glycerol, and 1 mM CHAPS, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 3
Reconstruction of Quaternary Structure from X-ray Scattering by Equilibrium Mixtures of Biological Macromolecules Biochemistry 52(39):6844-6855 (2013)
Petoukhov M, Billas I, Takacs M, Graewert M, Moras D, Svergun D
RgGuinier 4.3 nm
Dmax 13.2 nm

SASDM35 – Mixture of estrogen-related receptor gamma:Inverse repeat IR3 DNA - 6:3 and 2:1 complexes - at 1.0 mg/ml

Estrogen-related receptor gammaInverse repeat IR3 DNA experimental SAS data
SASREF MX model
Sample: Estrogen-related receptor gamma hexamer, 230 kDa Homo sapiens protein
Inverse repeat IR3 DNA trimer, 46 kDa DNA
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 100 mM KCl, 5 mM MgCl2, 1% (v/v) glycerol, and 1 mM CHAPS, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 3
Reconstruction of Quaternary Structure from X-ray Scattering by Equilibrium Mixtures of Biological Macromolecules Biochemistry 52(39):6844-6855 (2013)
Petoukhov M, Billas I, Takacs M, Graewert M, Moras D, Svergun D
RgGuinier 4.1 nm
Dmax 12.8 nm

SASDAN3 – MutS dimer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS dimer, 191 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Feb 28
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 4.7 nm
Dmax 15.5 nm
VolumePorod 307 nm3

SASDAQ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DAMMIF model
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 28.0 nm
VolumePorod 700 nm3

SASDAX3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.5 nm
Dmax 29.0 nm
VolumePorod 750 nm3

SASDAY3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.3 nm
Dmax 29.0 nm
VolumePorod 720 nm3

SASDAZ3 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 8.0 nm

SASDA24 – MutS tetramer

DNA mismatch repair protein MutS experimental SAS data
DNA mismatch repair protein MutS Kratky plot
Sample: DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer: 50 mM HEPES 50 mM KCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12
Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK
RgGuinier 7.8 nm
Dmax 27.0 nm

SASDA45 – PpoA wild type enzyme

Psi-producing oxygenase A experimental SAS data
SASREF model
Sample: Psi-producing oxygenase A trimer, 362 kDa Aspergillus nidulans protein
Buffer: 20 Mm HEPES, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Jun 24
A structural model of PpoA derived from SAXS-analysis-implications for substrate conversion. Biochim Biophys Acta 1831(9):1449-57 (2013)
Koch C, Tria G, Fielding AJ, Brodhun F, Valerius O, Feussner K, Braus GH, Svergun DI, Bennati M, Feussner I
RgGuinier 5.4 nm
Dmax 16.5 nm
VolumePorod 540 nm3

4338 hits found.