Browse by MODEL: Hybrid

SASDE67 – Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 6 mg/ml

Aldehyde dehydrogenase 16 from Loktanella sp. experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase 16 from Loktanella sp. dimer, 161 kDa Loktanella sp. 3ANDIMAR09 protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.5 nm
Dmax 10.6 nm
VolumePorod 207 nm3

SASDE77 – Aldehyde dehydrogenase 16 from Loktanella sp. (LsALDH16): 8 mg/ml

Aldehyde dehydrogenase 16 from Loktanella sp. experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase 16 from Loktanella sp. dimer, 161 kDa Loktanella sp. 3ANDIMAR09 protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.6 nm
Dmax 10.8 nm
VolumePorod 205 nm3

SASDE87 – Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1 mg/ml

Aldehyde dehydrogenase family 16 member A1 from Homo sapiens experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens dimer, 171 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.6 nm
Dmax 10.9 nm
VolumePorod 230 nm3

SASDE97 – Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 1.6 mg/ml

Aldehyde dehydrogenase family 16 member A1 from Homo sapiens experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens dimer, 171 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.2 nm
VolumePorod 236 nm3

SASDEA7 – Aldehyde dehydrogenase family 16 member A1 from Homo sapiens (HsALDH16A1): 3.2 mg/ml

Aldehyde dehydrogenase family 16 member A1 from Homo sapiens experimental SAS data
PYMOL model
Sample: Aldehyde dehydrogenase family 16 member A1 from Homo sapiens dimer, 171 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, 100 mM NaCl, 2.0% glycerol, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Dec 13
Crystal Structure of Aldehyde Dehydrogenase 16 Reveals Trans-Hierarchical Structural Similarity and a New Dimer. J Mol Biol (2018)
Liu LK, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.5 nm
VolumePorod 237 nm3

SASDDG2 – Glycosylated Human Immunoglobulin G Fc Region

Glycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Glycosylated human immunoglobulin G Fc region dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. MAbs (2018)
Yageta S, Imamura H, Shibuya R, Honda S
RgGuinier 2.7 nm
Dmax 10.2 nm
VolumePorod 66 nm3

SASDDH2 – Aglycosylated Human Immunoglobulin G Fc Region

Aglycosylated human immunoglobulin G Fc region experimental SAS data
MODELLER model
Sample: Aglycosylated human immunoglobulin G Fc region dimer, 51 kDa Homo sapiens protein
Buffer: 20 mM Citrate-Phosphate, pH: 7
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Mar 5
CH2 domain orientation of human immunoglobulin G in solution: Structural comparison of glycosylated and aglycosylated Fc regions using small-angle X-ray scattering. MAbs (2018)
Yageta S, Imamura H, Shibuya R, Honda S
RgGuinier 2.9 nm
Dmax 9.8 nm
VolumePorod 60 nm3

SASDDB8 – Periplasmic domain of inner membrane protein GspL, dimer

Type II secretion system protein L, periplasmic domain experimental SAS data
EOM/RANCH model
Sample: Type II secretion system protein L, periplasmic domain dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 50 mM TRIS, 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Apr 8
Structure and oligomerization of the periplasmic domain of GspL from the type II secretion system of Pseudomonas aeruginosa. Sci Rep 8(1):16760 (2018)
Fulara A, Vandenberghe I, Read RJ, Devreese B, Savvides SN
RgGuinier 2.2 nm
Dmax 7.5 nm

SASDEE2 – The N-terminal domain of estrogen receptor alpha

Estrogen receptor experimental SAS data
CUSTOM IN-HOUSE model
Sample: Estrogen receptor monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, 50 mM NaCl, 0.05 mM TCEP, pH: 7.4
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2017 Jun 12
A Metastable Contact and Structural Disorder in the Estrogen Receptor Transactivation Domain. Structure 27(2):229-240.e4 (2019)
Peng Y, Cao S, Kiselar J, Xiao X, Du Z, Hsieh A, Ko S, Chen Y, Agrawal P, Zheng W, Shi W, Jiang W, Yang L, Chance MR, Surewicz WK, Buck M, Yang S
RgGuinier 3.0 nm
Dmax 10.0 nm

SASDEN4 – Protein tyrosine phosphatase SHP2

Tyrosine-protein phosphatase non-receptor type 11 experimental SAS data
ALLOSMOD model
Sample: Tyrosine-protein phosphatase non-receptor type 11 monomer, 61 kDa Homo sapiens protein
Buffer: 50 mM ADA, 2 mM TCEP, pH: 6.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2016 Mar 28
Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2. Nat Commun 9(1):4507 (2018)
Pádua RAP, Sun Y, Marko I, Pitsawong W, Stiller JB, Otten R, Kern D
RgGuinier 2.7 nm
Dmax 8.9 nm