Browse by MODEL: Ab initio only

SASDBT9 – Full-length human βB2-crystallin

Beta-crystallin B2 experimental SAS data
DAMMIN model
Sample: Beta-crystallin B2 dimer, 46 kDa Homo sapiens protein
Buffer: 25 mM NaPi, 5 mM DTT, 1 mM EDTA,, pH: 6.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 20
Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure 25(3):496-505 (2017)
Xi Z, Whitley MJ, Gronenborn AM
RgGuinier 2.2 nm
Dmax 8.1 nm
VolumePorod 67 nm3

SASDBU9 – Terminally truncated human βB2-crystallin

Beta-crystallin B2 experimental SAS data
DAMMIN model
Sample: Beta-crystallin B2 dimer, 42 kDa Homo sapiens protein
Buffer: 25 mM NaPi, 5 mM DTT, 1 mM EDTA,, pH: 6.5
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2015 Mar 20
Human βB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study. Structure 25(3):496-505 (2017)
Xi Z, Whitley MJ, Gronenborn AM
RgGuinier 2.1 nm
Dmax 6.7 nm
VolumePorod 62 nm3

SASDBW9 – Immunoglobulin domains 4,5 of Nucleoporin Pom152 (Pom152 Ig-4,5: amino acids 718-920)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 24 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.7 nm
Dmax 9.4 nm
VolumePorod 23 nm3

SASDBX9 – Immunoglobulin domain 6 of Nucleoporin Pom152 (Pom152 Ig-6: amino acids 919-1020)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 57 nm3

SASDBY9 – Immunoglobulin domains 3,4 of Nucleoporin Pom152 (Pom152 Ig-3,4: amino acids 603-820)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 26 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 28 nm3

SASDBZ9 – Immunoglobulin domains 4,5,6,7 of Nucleoporin Pom152 (Pom152 Ig-4,5,6,7: amino acids 718-1148)

Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 49 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 4.3 nm
Dmax 15.4 nm
VolumePorod 67 nm3

SASDDJ7 – Citrate-binding PAS domain from the sensor histidine kinase, CitA, fused to lipase EstA

citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA experimental SAS data
DAMMIF model
Sample: Citrate-binding CitAP domain fused to lipase A of Bacillus subtilis BsLA dimer, 77 kDa protein
Buffer: 10 mM glycine buffer, 10 mM NaCl, pH: 10
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 6
A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase. Sci Rep 7:42592 (2017)
Kaschner M, Schillinger O, Fettweiss T, Nutschel C, Krause F, Fulton A, Strodel B, Stadler A, Jaeger KE, Krauss U
RgGuinier 3.3 nm
Dmax 11.8 nm

SASDAH7 – Metal-free hETHE1, 0.5 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 9.0 nm
Dmax 32.3 nm
VolumePorod 400 nm3

SASDAJ7 – Metal-free hETHE1, 1 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 8.3 nm
Dmax 38.0 nm
VolumePorod 602 nm3

SASDAK7 – Metal-free hETHE1, 2 mg/ml

Persulfide dioxygenase ETHE1, mitochondrial experimental SAS data
DAMMIN model
Sample: Persulfide dioxygenase ETHE1, mitochondrial dimer, 56 kDa Homo sapiens protein
Buffer: 50 mM Tris 150 mM NaCl 2 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 23
Distinctive features and structural significance of the Homo sapiens ethylmalonic encephalopathy protein iron binding site
Al Kikhney, Marco Salomone-Stagni
RgGuinier 8.8 nm
Dmax 42.5 nm
VolumePorod 647 nm3