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

SASDDC8 – Periplasmic domain of inner membrane protein GspL, tetramer

Type II secretion system protein L, periplasmic domain experimental SAS data
Type II secretion system protein L, periplasmic domain Kratky plot
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 3.2 nm
Dmax 10.5 nm

SASDEV4 – ACA8 protein (apo) in stealth nanodisc

Membrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl)Calcium-transporting ATPase 8, plasma membrane-type experimental SAS data
Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Calcium-transporting ATPase 8, plasma membrane-type Kratky plot
Sample: Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) , 1 kDa Escherichia coli
Calcium-transporting ATPase 8, plasma membrane-type monomer, 118 kDa Arabidopsis thaliana protein
Buffer: 30 mM Tris, 150 mM NaCl, 1mM MgCl2, 1 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 8
Structural basis for activation of plasma-membrane Ca2+-ATPase by calmodulin. Commun Biol 1:206 (2018)
Nitsche J, Josts I, Heidemann J, Mertens HD, Maric S, Moulin M, Haertlein M, Busch S, Forsyth VT, Svergun DI, Uetrecht C, Tidow H
RgGuinier 5.3 nm
Dmax 20.0 nm
VolumePorod 626 nm3

4736 hits found.