Browse by MODEL: Hybrid

SASDF75 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a) amino acids 1-452

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 51 kDa Bos taurus protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Structural underpinnings of Ric8A function as a G-protein α-subunit chaperone and guanine-nucleotide exchange factor. Nat Commun 10(1):3084 (2019)
Srivastava D, Gakhar L, Artemyev NO
RgGuinier 3.0 nm
Dmax 11.2 nm
VolumePorod 70 nm3

SASDED9 – Relaxase domain of TraI

Relaxase (Tra_2) domain of TraI experimental SAS data
GASBOR model
Sample: Relaxase (Tra_2) domain of TraI monomer, 46 kDa Neisseria gonorrhoeae protein
Buffer: 50 mM TRIS-HCl 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 11
DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island. Nucleic Acids Res 47(15):8136-8153 (2019)
Heilers JH, Reiners J, Heller EM, Golzer A, Smits SHJ, van der Does C
RgGuinier 2.6 nm
Dmax 8.3 nm
VolumePorod 61 nm3

SASDEE9 – TraI_2_C domain of TraI

TraI_2_C domain of TraI experimental SAS data
GASBOR model
Sample: TraI_2_C domain of TraI monomer, 21 kDa Neisseria gonorrhoeae protein
Buffer: 50 mM TRIS-HCl 100 mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 11
DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island. Nucleic Acids Res 47(15):8136-8153 (2019)
Heilers JH, Reiners J, Heller EM, Golzer A, Smits SHJ, van der Does C
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 40 nm3

SASDF93 – Ignicoccus islandicus malate dehydrogenase

Malate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Malate dehydrogenase tetramer, 134 kDa Ignicoccus islandicus DSM … protein
Buffer: 50 mM Tris-HCl 50 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 5
The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization Journal of Structural Biology (2019)
Roche J, Girard E, Mas C, Madern D
RgGuinier 3.3 nm
Dmax 9.0 nm
VolumePorod 198 nm3

SASDF94 – Insulin glulisine (Apidra), oligomeric composition

Insulin glulisine experimental SAS data
CUSTOM IN-HOUSE model
Sample: Insulin glulisine hexamer, 35 kDa protein
Buffer: Apidra formulation (per ml: 5 mg Sodium chloride, 3.15 mg m-Cresol, 6 mg Trometamol, 0.01 mg Polysorbate 20), pH: 7.3
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Apr 20
The quaternary structure of insulin glargine and glulisine under formulation conditions. Biophys Chem 253:106226 (2019)
Nagel N, Graewert MA, Gao M, Heyse W, Jeffries CM, Svergun D, Berchtold H
RgGuinier 2.3 nm
Dmax 7.6 nm

SASDFA4 – Insulin glargine (Toujeo®), oligomeric composition

Insulin glargine (Toujeo®) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Insulin glargine (Toujeo®) hexamer, 36 kDa protein
Buffer: Toujeo Fromulation (190 ug Zinc chloride, 2.7 mg m-Cresol, 20 mg glycerol 85%), pH: 4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Jul 5
The quaternary structure of insulin glargine and glulisine under formulation conditions. Biophys Chem 253:106226 (2019)
Nagel N, Graewert MA, Gao M, Heyse W, Jeffries CM, Svergun D, Berchtold H
RgGuinier 1.8 nm
Dmax 6.2 nm

SASDEL9 – Escherichia coli aerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaFatty acid oxidation complex subunit alpha3-ketoacyl-CoA thiolase FadA (beta subunit) experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
Fatty acid oxidation complex subunit alpha monomer, 81 kDa Escherichia coli protein
3-ketoacyl-CoA thiolase FadA (beta subunit) dimer, 82 kDa Escherichia coli protein
Buffer: 20 mM 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid (HEPES), 120 mM KCl, 2.5 mM DTT, pH: 7.2
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 May 30
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 406 nm3

SASDEM9 – anEcTFE: Escherichia coli anaerobic fatty acid beta-oxidation trifunctional enzyme complex

Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic Fatty acid oxidation complex subunit alphaanaerobic 3-ketoacyl-CoA thiolase FadI beta subunitanaerobic 3-ketoacyl-CoA thiolase FadI beta subunit experimental SAS data
DAMMIN model
Sample: Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli (strain … protein
Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
Anaerobic Fatty acid oxidation complex subunit alpha monomer, 77 kDa Escherichia coli protein
Anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
Anaerobic 3-ketoacyl-CoA thiolase FadI beta subunit dimer, 96 kDa Escherichia coli protein
Buffer: 50 mM Tris, 500 mM NaCl, 5% glycerol, 0.05% C12E9 (1-O-(n-Dodecyl)-nonaethyleneglycol), 2.5 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 22
Complementary substrate specificity and distinct quaternary assembly of the Escherichia coli aerobic and anaerobic beta-oxidation trifunctional enzyme complexes. Biochem J (2019)
Sah-Teli SK, Hynönen MJ, Schmitz W, Geraets JA, Seitsonen J, Pedersen JS, Butcher SJ, Wierenga RK, Venkatesan R
RgGuinier 6.2 nm
Dmax 19.6 nm
VolumePorod 856 nm3

SASDFM5 – Mutant 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, H110A tetramer, at pH 8.5

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 50 mM Tris, 5 mM DTT, pH: 8.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jul 15
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem 294(30):11609-11621 (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 5.2 nm
Dmax 19.0 nm
VolumePorod 238 nm3

SASDFN5 – Wild type 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase, ACMSD tetramer, at pH 7.0

2-amino-3-carboxymuconate 6-semialdehyde decarboxylase experimental SAS data
CORAL model
Sample: 2-amino-3-carboxymuconate 6-semialdehyde decarboxylase tetramer, 159 kDa Pseudomonas fluorescens protein
Buffer: 25 mM HEPES, 5 mM DTT, pH: 7
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2018 Jan 10
Quaternary structure of α-amino-β-carboxymuconate-ϵ-semialdehyde decarboxylase (ACMSD) controls its activity. J Biol Chem 294(30):11609-11621 (2019)
Yang Y, Davis I, Matsui T, Rubalcava I, Liu A
RgGuinier 4.7 nm
Dmax 17.5 nm
VolumePorod 195 nm3