|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|
|
|
|
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 |
|
|