Browse by ORGANISM: other species

SASDBV5 – Cyclopentadecanone monooxygenase, NADP+, wild-type

Cyclopentadecanone 1,2-monooxygenase experimental SAS data
Cyclopentadecanone 1,2-monooxygenase Kratky plot
Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer: 50 mM Tris 2 mM TCEP 5 mM NADP+, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.7 nm
Dmax 8.7 nm
VolumePorod 120 nm3

SASDBW5 – Cyclopentadecanone monooxygenase, NADP+ and cyclopentadecanone, wild-type

Cyclopentadecanone 1,2-monooxygenase experimental SAS data
Cyclopentadecanone 1,2-monooxygenase Kratky plot
Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer: 50mM Tris 2mM TCEP 5mM NADP+ 1mM cyclopentadecanon, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 110 nm3

SASDBX5 – Cyclopentadecanone monooxygenase, NADP+ and ω-pentadecalactone, wild-type

Cyclopentadecanone 1,2-monooxygenase experimental SAS data
Cyclopentadecanone 1,2-monooxygenase Kratky plot
Sample: Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
Buffer: 50mM Tris mM TCEP 5mM NADP+ 1mM ω-pentadecalactone, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Oct 2
The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure. Biochim Biophys Acta 1864(12):1641-1648 (2016)
Yachnin BJ, Lau PCK, Berghuis AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 100 nm3

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