SASDBC6 – Compound 6:BRD4 (2:1)

Bromodomain-containing protein 4 experimental SAS data
DAMMIF model
Sample: Bromodomain-containing protein 4 monomer, 56 kDa Homo sapiens protein
Buffer: 20mM Hepes, 100mM NaCl, 1mM Tris(2-carboxyethyl)phosphine hydrochloride, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2015 Feb 8
Potent and selective bivalent inhibitors of BET bromodomains. Nat Chem Biol 12(12):1097-1104 (2016)
Waring MJ, Chen H, Rabow AA, Walker G, Bobby R, Boiko S, Bradbury RH, Callis R, Clark E, Dale I, Daniels DL, Dulak A, Flavell L, Holdgate G, Jowitt TA, Kikhney A, McAlister M, Méndez J, Ogg D, Patel J...
RgGuinier 4.4 nm
Dmax 17.3 nm

SASDB27 – Chimeric EcRHH-RcPutA: The E.coli Proline utilization A RHH domain fused to R.capsulatus PutA

Proline utilization A experimental SAS data
Proline utilization A Kratky plot
Sample: Proline utilization A dimer, 251 kDa Escherchia coli, Rhodobacter … protein
Buffer: 50 mM Tris, 200 mM NaCl, 0.5 mM Tris(3-hydroxypropyl)phosphine, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 16
Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA. Biosci Rep 36(6) (2016)
Arentson BW, Hayes EL, Zhu W, Singh H, Tanner JJ, Becker DF
RgGuinier 5.2 nm
Dmax 18.3 nm
VolumePorod 308 nm3

SASDBK7 – Vaccinia virus A46 protein (full-length)

Protein A46 experimental SAS data
CORAL model
Sample: Protein A46 tetramer, 112 kDa Vaccinia virus protein
Buffer: 20 mM Tris-HCl, 10 mM DTT, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Jun 25
Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins. PLoS Pathog 12(12):e1006079 (2016)
Fedosyuk S, Bezerra GA, Radakovics K, Smith TK, Sammito M, Bobik N, Round A, Ten Eyck LF, Djinović-Carugo K, Usón I, Skern T
RgGuinier 4.3 nm
Dmax 14.0 nm
VolumePorod 199 nm3

SASDBL7 – N-terminal domain of Vaccinia virus A46 protein (1-83)

Protein A46 experimental SAS data
CORAL model
Sample: Protein A46 tetramer, 40 kDa Vaccinia virus protein
Buffer: 20 mM Tris-HCl, 10 mM DTT, pH: 8.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Jun 25
Vaccinia Virus Immunomodulator A46: A Lipid and Protein-Binding Scaffold for Sequestering Host TIR-Domain Proteins. PLoS Pathog 12(12):e1006079 (2016)
Fedosyuk S, Bezerra GA, Radakovics K, Smith TK, Sammito M, Bobik N, Round A, Ten Eyck LF, Djinović-Carugo K, Usón I, Skern T
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 68 nm3

SASDLN4 – Insomniac protein (INC) – cullin 3 complex

Cullin 3Insomniac protein experimental SAS data
SASREF model
Sample: Cullin 3 pentamer, 60 kDa Drosophila melanogaster protein
Insomniac protein pentamer, 210 kDa Drosophila melanogaster protein
Buffer: 50 mM TrisHCl, 300 mM NaCl, 2 mM DTT, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2014 Nov 24
Proteins involved in sleep homeostasis: Biophysical characterization of INC and its partners Biochimie 131:106-114 (2016)
Pirone L, Smaldone G, Esposito C, Balasco N, Petoukhov M, Spilotros A, Svergun D, Di Gaetano S, Vitagliano L, Pedone E
RgGuinier 6.7 nm
Dmax 25.2 nm

SASDDL2 – Sinorhizobium meliloti Proline Utilization A (PutA) lowest concentration, 1.00 mg/ml

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 171 nm3

SASDDM2 – Sinorhizobium meliloti Proline Utilization A (PutA) at 2.00 mg/ml

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.9 nm
VolumePorod 225 nm3

SASDDN2 – Sinorhizobium meliloti Proline Utilization A (PutA) at 3.00 mg/ml

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.8 nm
Dmax 11.8 nm
VolumePorod 248 nm3

SASDDP2 – Sinorhizobium meliloti Proline Utilization A (PutA) at high concentration, 4.00 mg/ml

Sinorhizobium meliloti (SmPutA) experimental SAS data
MES-FOXS model
Sample: Sinorhizobium meliloti (SmPutA) monomer, 132 kDa Sinorhizobium meliloti protein
Buffer: 50 mM Tris, 1% (v/v) glycerol, 0.5 mM THP, and 50 mM NaCl, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Mar 27
Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function. J Biol Chem 291(46):24065-24075 (2016)
Luo M, Gamage TT, Arentson BW, Schlasner KN, Becker DF, Tanner JJ
RgGuinier 3.9 nm
Dmax 11.9 nm
VolumePorod 277 nm3

SASDBZ5 – Enzyme I-Ntr (residues 170-424) in complex with NPr (residues 1-85)

Phosphocarrier protein NPrPhosphoenolpyruvate-protein phosphotransferase PtsP experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Phosphocarrier protein NPr monomer, 9 kDa Escherichia coli protein
Phosphoenolpyruvate-protein phosphotransferase PtsP monomer, 28 kDa Escherichia coli protein
Buffer: 10 mM Tris 150 mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2015 Jan 30
Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. Structure 24(12):2127-2137 (2016)
Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N
RgGuinier 2.3 nm
Dmax 8.2 nm
VolumePorod 52 nm3

4774 hits found.