|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris 5 mM NADP+, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15
|
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 |
9.2 |
nm |
| VolumePorod |
100 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15
|
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 |
3.0 |
nm |
| Dmax |
10.1 |
nm |
| VolumePorod |
120 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris 5 mM NADP+, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15
|
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 |
3.0 |
nm |
| Dmax |
11.0 |
nm |
| VolumePorod |
130 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
|
| Buffer: |
50 mM Tris 5 mM NADP+, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Jul 15
|
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 |
2.8 |
nm |
| Dmax |
9.2 |
nm |
| VolumePorod |
110 |
nm3 |
|
|
|
|
|
|
|
| Sample: |
Cyclopentadecanone 1,2-monooxygenase monomer, 68 kDa Pseudomonas sp. HI-70 protein
|
| Buffer: |
50 mM Tris 2 mM TCEP, pH: 8 |
| Experiment: |
SAXS
data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Jan 27
|
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 |
2.8 |
nm |
| Dmax |
10.4 |
nm |
| VolumePorod |
110 |
nm3 |
|
|
|
|
|
|
|
| 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 |
|
|
|
|
|
|
|
| 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 |
|
|
|
|
|
|
|
| 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 |
|
|
|
|
|
|
|
| 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 |
|
|
|
|
|
|
|
| Sample: |
AIR-3A 2'FU dimer, 13 kDa RNA
|
| Buffer: |
water, pH: 7.5 |
| Experiment: |
SAXS
data collected at EMBL P12, PETRA III on 2013 Dec 6
|
Structure and target interaction of a G-quadruplex RNA-aptamer.
RNA Biol 13(10):973-987 (2016)
Szameit K, Berg K, Kruspe S, Valentini E, Magbanua E, Kwiatkowski M, Chauvot de Beauchêne I, Krichel B, Schamoni K, Uetrecht C, Svergun DI, Schlüter H, Zacharias M, Hahn U
|
| RgGuinier |
1.9 |
nm |
| Dmax |
6.0 |
nm |
| VolumePorod |
12 |
nm3 |
|
|