Browse by ORGANISM: other species

SASDC58 – Dipeptidyl peptidase III: pgDPP3_FL

Peptidase, M49 family experimental SAS data
DAMMIN model
Sample: Peptidase, M49 family monomer, 102 kDa Porphyromonas gingivalis protein
Buffer: 50mM Tris,100mM NaCl, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 14
A novel Porphyromonas gingivalis enzyme: An atypical dipeptidyl peptidase III with an ARM repeat domain. PLoS One 12(11):e0188915 (2017)
Hromić-Jahjefendić A, Jajčanin Jozić N, Kazazić S, Grabar Branilović M, Karačić Z, Schrittwieser JH, Das KMP, Tomin M, Oberer M, Gruber K, Abramić M, Tomić S
RgGuinier 3.0 nm
Dmax 11.3 nm
VolumePorod 116 nm3

SASDBA5 – Cyclohexanone monooxygenase, wild-type

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 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 9.3 nm
VolumePorod 110 nm3

SASDBB5 – Cyclohexanone monooxygenase, NADP+, wild-type

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 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 2.6 nm
Dmax 8.0 nm
VolumePorod 99 nm3

SASDBC5 – Cyclohexanone monooxygenase, NADP+ and cyclohexanone, wild-type

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 cyclohexanone, 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 2.5 nm
Dmax 7.8 nm
VolumePorod 100 nm3

SASDBD5 – Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, wild-type

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 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 2.5 nm
Dmax 7.5 nm
VolumePorod 99 nm3

SASDBE5 – Cyclohexanone monooxygenase, W492A

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 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 2.8 nm
Dmax 9.5 nm
VolumePorod 110 nm3

SASDBF5 – Cyclohexanone monooxygenase, NADP+, K501A

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 8.7 nm
VolumePorod 100 nm3

SASDBG5 – Cyclohexanone monooxygenase, NADP+, W492A

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 cyclohexanone, 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 8.9 nm
VolumePorod 96 nm3

SASDBH5 – Cyclohexanone monooxygenase, NADP+ and cyclohexanone, W492A

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 cyclohexanone, 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 8.9 nm
VolumePorod 98 nm3

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

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