Browse by MODEL: Ab initio only

SASDC54 – Envelope of Col H PKD-PKD-CBD complexed with mini-collagen

ColH proteinCollagenous Peptide model [(PPG)10] experimental SAS data
DAMMIF model
Sample: ColH protein monomer, 34 kDa Hathewaya histolytica protein
Collagenous Peptide model [(PPG)10] trimer, 10 kDa synthetic construct protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 3.3 nm
Dmax 14.2 nm
VolumePorod 38 nm3

SASDC64 – Envelope of Col G PKD-CBD-CBD complexed with mini-collagen

Collagenous Peptide model [(PPG)10]ColG Collagenase experimental SAS data
DAMMIF model
Sample: Collagenous Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
ColG Collagenase monomer, 37 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 4.1 nm
Dmax 19.3 nm
VolumePorod 70 nm3

SASDDP9 – C-terminal half of pseudorabies virus tegument protein UL37

Tegument protein UL37 experimental SAS data
DAMMIN model
Sample: Tegument protein UL37 monomer, 49 kDa Suid alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 71 nm3

SASDDQ9 – N-terminal half of herpes simplex virus type-1 inner tegument protein UL37

Inner tegument protein experimental SAS data
DAMFILT model
Sample: Inner tegument protein monomer, 62 kDa Human alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 3.3 nm
Dmax 10.4 nm
VolumePorod 91 nm3

SASDEL4 – Residues 478-884 of pseudorabies virus tegument protein UL37

Tegument protein UL37 experimental SAS data
DAMMIN model
Sample: Tegument protein UL37 monomer, 43 kDa Suid alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 3.9 nm
Dmax 12.5 nm

SASDD99 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M NaCl

VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M NaCl, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.4 nm
Dmax 7.7 nm
VolumePorod 63 nm3

SASDDA9 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M KBr

VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M KBr, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.3 nm
Dmax 7.7 nm
VolumePorod 46 nm3

SASDDB9 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M NaBr

VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M NaBr, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 26
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.5 nm
Dmax 8.1 nm
VolumePorod 59 nm3

SASDDC9 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M RbCl

VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M RbCl, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 3.3 nm
Dmax 9.3 nm
VolumePorod 89 nm3

SASDDW4 – Procollagen lysyl hydroxylase LH3 measured using SEC-SAXS

Procollagen lysyl hydroxylase LH3 experimental SAS data
GASBOR model
Sample: Procollagen lysyl hydroxylase LH3 dimer, 180 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 200 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Feb 28
Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3. Nat Commun 9(1):3163 (2018)
Scietti L, Chiapparino A, De Giorgi F, Fumagalli M, Khoriauli L, Nergadze S, Basu S, Olieric V, Cucca L, Banushi B, Profumo A, Giulotto E, Gissen P, Forneris F
RgGuinier 5.1 nm
Dmax 21.0 nm
VolumePorod 268 nm3