SASBDB entries for UniProt ID:

SASDBJ5 – Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, W492A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
Sample: Cyclohexanone monooxygenase monomer, 61 kDa Rhodococcus sp. HI-31 protein
Buffer: 50 mM Tris 5 mM NADP+ 5 mM ε-caprolactone, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2014 Feb 25
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

SASDBK5 – Cyclohexanone monooxygenase, K328A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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 2.8 nm
Dmax 9.8 nm
VolumePorod 110 nm3

SASDBL5 – Cyclohexanone monooxygenase, NADP+, K328A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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 2.6 nm
Dmax 8.4 nm
VolumePorod 100 nm3

SASDBM5 – Cyclohexanone monooxygenase, K328A-W492A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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 Nov 17
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 9.4 nm
VolumePorod 110 nm3

SASDBN5 – Cyclohexanone monooxygenase, NADP+, K328A-W492A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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 Nov 17
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 7.8 nm
VolumePorod 96 nm3

SASDBP5 – Cyclohexanone monooxygenase, N497A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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 2.9 nm
Dmax 10.4 nm
VolumePorod 120 nm3

SASDBQ5 – Cyclohexanone monooxygenase, NADP+, N497A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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

SASDBR5 – Cyclohexanone monooxygenase, K501A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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

SASDBS5 – Cyclohexanone monooxygenase, N497A-K501A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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

SASDBT5 – Cyclohexanone monooxygenase, NADP+, N497A-K501A

UniProt ID: C0STX7 (None-None) Cyclohexanone monooxygenase
Cyclohexanone monooxygenase experimental SAS data
Cyclohexanone monooxygenase Kratky plot
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