Browse by ORGANISM: Homo sapiens (Human)

SASDCT2 – Bromodomain-containing protein 2 (BRD2) tandem bromodomains

Bromodomain-containing protein 2 experimental SAS data
DAMMIN model
Sample: Bromodomain-containing protein 2 monomer, 43 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jan 13
Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains. Mol Cell (2018)
Lambert JP, Picaud S, Fujisawa T, Hou H, Savitsky P, Uusküla-Reimand L, Gupta GD, Abdouni H, Lin ZY, Tucholska M, Knight JDR, Gonzalez-Badillo B, St-Denis N, Newman JA, Stucki M, Pelletier L, Bandeira N, Wilson MD, Filippakopoulos P, Gingras AC
RgGuinier 5.7 nm
Dmax 21.0 nm
VolumePorod 220 nm3

SASDCU2 – Bromodomain testis-specific protein (BRDT) tandem bromodomains

Bromodomain testis-specific protein experimental SAS data
DAMMIN model
Sample: Bromodomain testis-specific protein monomer, 43 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2% glycerol, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jan 13
Interactome Rewiring Following Pharmacological Targeting of BET Bromodomains. Mol Cell (2018)
Lambert JP, Picaud S, Fujisawa T, Hou H, Savitsky P, Uusküla-Reimand L, Gupta GD, Abdouni H, Lin ZY, Tucholska M, Knight JDR, Gonzalez-Badillo B, St-Denis N, Newman JA, Stucki M, Pelletier L, Bandeira N, Wilson MD, Filippakopoulos P, Gingras AC
RgGuinier 5.1 nm
Dmax 20.0 nm
VolumePorod 200 nm3

SASDEZ6 – Gamma-crystallin S disulfide-linked dimer

Gamma-crystallin S experimental SAS data
DAMMIN model
Sample: Gamma-crystallin S dimer, 42 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23
The structure and stability of the disulfide-linked γS-crystallin dimer provide insight into oxidation products associated with lens cataract formation. J Mol Biol (2018)
Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA
RgGuinier 2.4 nm
Dmax 7.5 nm
VolumePorod 45 nm3

SASDE27 – Gamma-crystallin S monomer

Gamma-crystallin S experimental SAS data
CHIMERA model
Sample: Gamma-crystallin S monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM sodium phosphate, pH: 7
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2018 Feb 23
The structure and stability of the disulfide-linked γS-crystallin dimer provide insight into oxidation products associated with lens cataract formation. J Mol Biol (2018)
Thorn DC, Grosas AB, Mabbitt PD, Ray NJ, Jackson CJ, Carver JA
RgGuinier 1.8 nm
Dmax 5.9 nm
VolumePorod 27 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

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