Browse by DISSEMINATION: Published

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

SASDAJ4 – CRM1

Exportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 3.8 nm
Dmax 11.0 nm
VolumePorod 190 nm3

SASDAK4 – CRM1 RanGTP

Exportin-1GTP-binding nuclear protein Ran experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 3.6 nm
Dmax 10.0 nm

SASDAL4 – CRM1 RanGTP Snu1

Exportin-1GTP-binding nuclear protein RanSnurportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
GTP-binding nuclear protein Ran monomer, 24 kDa Homo sapiens protein
Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Feb 3
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 4.1 nm
Dmax 14.0 nm

SASDAM4 – CRM1 Snu1

Exportin-1Snurportin-1 experimental SAS data
DAMMIF model
Sample: Exportin-1 monomer, 123 kDa Mus musculus protein
Snurportin-1 monomer, 41 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Dec 10
Structural determinants and mechanism of mammalian CRM1 allostery. Structure 21(8):1350-60 (2013)
Dölker N, Blanchet CE, Voß B, Haselbach D, Kappel C, Monecke T, Svergun DI, Stark H, Ficner R, Zachariae U, Grubmüller H, Dickmanns A
RgGuinier 4.3 nm
Dmax 15.0 nm

SASDLV4 – Ceruloplasmin ternary complex with lactoferrin and myeloperoxidase

CeruloplasminLactotransferrinMyeloperoxidase experimental SAS data
OTHER [STATIC IMAGE] model
Sample: Ceruloplasmin dimer, 244 kDa Homo sapiens protein
Lactotransferrin dimer, 156 kDa Homo sapiens protein
Myeloperoxidase dimer, 132 kDa Homo sapiens protein
Buffer: 0.1 M sodium-acetate buffer, pH: 5.6
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Nov 24
Ceruloplasmin: Macromolecular Assemblies with Iron-Containing Acute Phase Proteins PLoS ONE 8(7):e67145 (2013)
Samygina V, Sokolov A, Bourenkov G, Petoukhov M, Pulina M, Zakharova E, Vasilyev V, Bartunik H, Svergun D, Tuma R
RgGuinier 6.9 nm
Dmax 22.6 nm
VolumePorod 726 nm3