SASBDB entries for UniProt ID:

SASDH62 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08

UniProt ID: Q9EQZ6-3 (1-993) Isoform 3 of Rap guanine nucleotide exchange factor 4
Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2F-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 7
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.2 nm
Dmax 10.7 nm
VolumePorod 123 nm3

SASDH72 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08

UniProt ID: Q9EQZ6-3 (1-993) Isoform 3 of Rap guanine nucleotide exchange factor 4
Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2G-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 8
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 151 nm3

SASDH82 – Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08

UniProt ID: Q9EQZ6-3 (1-993) Isoform 3 of Rap guanine nucleotide exchange factor 4
Isoform 3 of Rap guanine nucleotide exchange factor 4 experimental SAS data
Isoform 3 of Rap guanine nucleotide exchange factor 4, aE2W-DB08 Rg histogram
Sample: Isoform 3 of Rap guanine nucleotide exchange factor 4 monomer, 114 kDa Mus musculus protein
Buffer: 150 mM NaCl, 1 mM EDTA, 1 mM DTT, and 10 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2008 Aug 11
Mechanism of Epac activation: structural and functional analyses of Epac2 hinge mutants with constitutive and reduced activities. J Biol Chem 284(35):23644-51 (2009)
Tsalkova T, Blumenthal DK, Mei FC, White MA, Cheng X
RgGuinier 3.6 nm
Dmax 11.4 nm
VolumePorod 145 nm3

SASDH92 – Plasmodium falciparum lipocalin (PF3D7_0925900): Dimer-tetramer equilibrium through a concentration series (combined batch and SEC-SAXS measurements)

UniProt ID: Q8I2Q0 (22-217) Plasmodium falciparum Lipocalin
Plasmodium falciparum Lipocalin experimental SAS data
SASREF MX model
Sample: Plasmodium falciparum Lipocalin tetramer, 89 kDa Plasmodium falciparum protein
Buffer: 20 mM Tris pH7.5, 150 mM NaCl, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Apr 8
Structure-Based Identification and Functional Characterization of a Lipocalin in the Malaria Parasite Plasmodium falciparum Cell Reports 31(12):107817 (2020)
Burda P, Crosskey T, Lauk K, Zurborg A, Söhnchen C, Liffner B, Wilcke L, Pietsch E, Strauss J, Jeffries C, Svergun D, Wilson D, Wilmanns M, Gilberger T
RgGuinier 3.2 nm
Dmax 10.3 nm
VolumePorod 126 nm3

SASDHA2 – Soluble guanylate cyclase (unbound)

UniProt ID: O77105 (1-699) Soluble guanylyl cyclase alpha-1 subunit

UniProt ID: O77106 (1-600) Soluble guanylyl cyclase beta-1 subunit
Soluble guanylyl cyclase alpha-1 subunitSoluble guanylyl cyclase beta-1 subunit experimental SAS data
BILBOMD model
Sample: Soluble guanylyl cyclase alpha-1 subunit monomer, 78 kDa Manduca sexta protein
Soluble guanylyl cyclase beta-1 subunit monomer, 68 kDa Manduca sexta protein
Buffer: 50 mM KH2PO4, 150 mM NaCl, 2% glycerol,, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 3
Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. Elife 8 (2019)
Horst BG, Yokom AL, Rosenberg DJ, Morris KL, Hammel M, Hurley JH, Marletta MA
RgGuinier 4.3 nm
Dmax 13.3 nm
VolumePorod 230 nm3

SASDHB2 – Soluble guanylate cyclase (nitric oxide, NO, bound)

UniProt ID: O77105 (1-699) Soluble guanylyl cyclase alpha-1 subunit

UniProt ID: O77106 (1-600) Soluble guanylyl cyclase beta-1 subunit
Soluble guanylyl cyclase alpha-1 subunitSoluble guanylyl cyclase beta-1 subunit experimental SAS data
BILBOMD model
Sample: Soluble guanylyl cyclase alpha-1 subunit monomer, 78 kDa Manduca sexta protein
Soluble guanylyl cyclase beta-1 subunit monomer, 68 kDa Manduca sexta protein
Buffer: 50 mM KH2PO4,150 mM NaCl, 2% glycerol, 500 µM NO,, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 3
Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. Elife 8 (2019)
Horst BG, Yokom AL, Rosenberg DJ, Morris KL, Hammel M, Hurley JH, Marletta MA
RgGuinier 4.4 nm
Dmax 14.2 nm
VolumePorod 218 nm3

SASDHC2 – PieE-FAD: 2,4-dichlorophenol 6-monooxygenase bound to flavin adenine dinucleotide

UniProt ID: W0C4C9 (1-598) 2,4-dichlorophenol 6-monooxygenase

UniProt ID: None (None-None) Flavin adenine dinucleotide
2,4-dichlorophenol 6-monooxygenaseFlavin adenine dinucleotide experimental SAS data
DAMMIN model
Sample: 2,4-dichlorophenol 6-monooxygenase hexamer, 399 kDa Streptomyces sp. SCSIO … protein
Flavin adenine dinucleotide hexamer, 5 kDa
Buffer: 20 mM Tris, 150 mM NaCl, 5 mM DTT, 2% glycerol, pH: 7.5
Experiment: SAXS data collected at Xenocs BioXolver L with MetalJet, Département de Biochimie, Université de Montréal on 2019 Oct 22
Structural analyses of the group A flavin-dependent monooxygenase PieE reveal a sliding FAD cofactor conformation bridging OUT and IN conformations. J Biol Chem (2020)
Manenda MS, Picard MÈ, Zhang L, Cyr N, Zhu X, Barma J, Pascal JM, Couture M, Zhang C, Shi R
RgGuinier 4.8 nm
Dmax 13.2 nm
VolumePorod 624 nm3

SASDHD2 – Urate Oxidase (Uricase) from Aspergillus flavus, measured by SEC-SAXS

UniProt ID: Q00511 (1-302) Urate Oxidase (Uricase) from Aspergillus flavus
Urate Oxidase (Uricase) from Aspergillus flavus experimental SAS data
CORAL model
Sample: Urate Oxidase (Uricase) from Aspergillus flavus tetramer, 137 kDa Aspergillus flavus protein
Buffer: 20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2019 Jul 1
Urate Oxidase (Uricase) from Aspergillus flavus
Tsutomu Matsui
RgGuinier 3.3 nm
Dmax 9.3 nm
VolumePorod 225 nm3

SASDHE2 – Type 1 insulin-like growth factor receptor ectodomains (IGF-1RΔβ)

UniProt ID: P08069 (31-935) Insulin-like growth factor 1 receptor
Insulin-like growth factor 1 receptor experimental SAS data
BUNCH model
Sample: Insulin-like growth factor 1 receptor dimer, 202 kDa Homo sapiens protein
Buffer: 30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Apr 22
Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformational change. J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC
RgGuinier 5.1 nm
Dmax 16.0 nm
VolumePorod 357 nm3

SASDHF2 – Insulin receptor ectodomains (IRΔβ)

UniProt ID: P06213-1 (28-948) Insulin receptor
Insulin receptor experimental SAS data
BUNCH model
Sample: Insulin receptor dimer, 203 kDa Homo sapiens protein
Buffer: 30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Dec 7
Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformational change. J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC
RgGuinier 5.5 nm
Dmax 17.0 nm
VolumePorod 385 nm3