SASBDB entries for UniProt ID:

SASDDW3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 2 mg/ml of Wild-type C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase, reductase component
p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.8 nm
Dmax 8.7 nm
VolumePorod 85 nm3

SASDDX3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 4 mg/ml of Wild-type C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase, reductase component
p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.7 nm
Dmax 8.6 nm
VolumePorod 95 nm3

SASDDY3 – p-hydroxyphenylacetate 3-hydroxylase, reductase component: 8 mg/ml of Wild-type C1 in 1 mM of p-hydroxyphenylacetic acid (HPA)

UniProt ID: Q6Q271 (None-None) p-hydroxyphenylacetate 3-hydroxylase, reductase component
p-hydroxyphenylacetate 3-hydroxylase, reductase component experimental SAS data
p-hydroxyphenylacetate 3-hydroxylase, reductase component Kratky plot
Sample: P-hydroxyphenylacetate 3-hydroxylase, reductase component dimer, 71 kDa Acinetobacter baumannii protein
Buffer: 50 mM MOPS, 0.5 mM EDTA, 1 mM DTT, 5% glycerol, 1 mM HPA, pH: 7
Experiment: SAXS data collected at BL1.3W, Synchrotron Light Research Institute (SLRI) on 2017 Mar 7
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands. Arch Biochem Biophys 653:24-38 (2018)
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
RgGuinier 2.7 nm
Dmax 8.9 nm
VolumePorod 102 nm3

SASDDQ4 – LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) of Insulin gene enhancer protein ISL-2

UniProt ID: P53776 (24-149) LIM/homeobox protein Lhx4

UniProt ID: Q9CXV0 (273-301) Insulin gene enhancer protein ISL-2
LIM/homeobox protein Lhx4Insulin gene enhancer protein ISL-2 experimental SAS data
DAMMIN model
Sample: LIM/homeobox protein Lhx4 monomer, 15 kDa Mus musculus protein
Insulin gene enhancer protein ISL-2 monomer, 4 kDa Mus musculus protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Nov 19
Mutation in a flexible linker modulates binding affinity for modular complexes. Proteins (2019)
Stokes PH, Robertson NO, Silva AP, Estephan T, Trewhella J, Guss JM, Matthews JM
RgGuinier 2.2 nm
Dmax 8.0 nm
VolumePorod 20 nm3

SASDDR4 – LIM/homeobox protein Lhx4 LIM domains fused to the LIM interaction domain (LID) R282G mutant of Insulin gene enhancer protein ISL-2

UniProt ID: P53776 (24-149) LIM/homeobox protein Lhx4

UniProt ID: Q9CXV0 (273-301) Insulin gene enhancer protein ISL-2 (R282G)
LIM/homeobox protein Lhx4Insulin gene enhancer protein ISL-2 (R282G) experimental SAS data
DAMMIN model
Sample: LIM/homeobox protein Lhx4 monomer, 15 kDa Mus musculus protein
Insulin gene enhancer protein ISL-2 (R282G) monomer, 4 kDa Mus musculus protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Nov 19
Mutation in a flexible linker modulates binding affinity for modular complexes. Proteins (2019)
Stokes PH, Robertson NO, Silva AP, Estephan T, Trewhella J, Guss JM, Matthews JM
RgGuinier 2.3 nm
Dmax 8.5 nm
VolumePorod 21 nm3

SASDDS4 – cGMP-dependent protein kinase 1: ∆53 PKG Iα

UniProt ID: P00516 (54-671) cGMP-dependent protein kinase 1
cGMP-dependent protein kinase 1 experimental SAS data
DAMFILT model
Sample: CGMP-dependent protein kinase 1 monomer, 70 kDa Bos taurus protein
Buffer: 50 mM MES, 300 mM NaCl, 1 mM TCEP, 5 mM DTT, pH: 6.9
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Jun 6
An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric and autoinhibited and provides a model for activation. J Biol Chem 293(21):7916-7929 (2018)
Moon TM, Sheehe JL, Nukareddy P, Nausch LW, Wohlfahrt J, Matthews DE, Blumenthal DK, Dostmann WR
RgGuinier 3.0 nm
Dmax 9.7 nm
VolumePorod 105 nm3

SASDDT4 – Fc region of Immunoglobulin G1 (IgG1 Fc)

UniProt ID: P01857 (None-None) Immunoglobulin heavy constant gamma 1
Immunoglobulin heavy constant gamma 1 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 dimer, 53 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.6 nm
Dmax 10.0 nm
VolumePorod 70 nm3

SASDDU4 – Fc region of Immunoglobulin G2 (IgG2 Fc)

UniProt ID: P01859 (None-None) Immunoglobulin heavy constant gamma 2
Immunoglobulin heavy constant gamma 2 experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 2 dimer, 52 kDa Homo sapiens protein
Buffer: 20mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.8 nm
Dmax 9.0 nm
VolumePorod 67 nm3

SASDDV4 – Fc-region of Immunoglobulin G1, M135Y/S137T/T139E mutant (IgG1 Fc-YTE)

UniProt ID: P01857 (None-None) Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E
Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E experimental SAS data
BILBOMD model
Sample: Immunoglobulin heavy constant gamma 1 M255Y/S257T/T259E dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 50mM NaCl, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Feb 17
Conformational Plasticity of the Immunoglobulin Fc Domain in Solution. Structure 26(7):1007-1014.e2 (2018)
Remesh SG, Armstrong AA, Mahan AD, Luo J, Hammel M
RgGuinier 2.7 nm
Dmax 10.0 nm
VolumePorod 74 nm3

SASDDW4 – Procollagen lysyl hydroxylase LH3 measured using SEC-SAXS

UniProt ID: O60568 (25-738) Procollagen lysyl hydroxylase LH3
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