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32 hits found for Yachnin

SASDLD2 – Circular permutant Carboxypeptidase G2-CP-N89-K177A

Carboxypeptidase G2 (circular permutant CP-N89) K177A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Carboxypeptidase G2 (circular permutant CP-N89) K177A dimer, 85 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jun 6
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 105 nm3

SASDLE2 – Circular permutant Carboxypeptidase G2-CP-N89-K177A with methotrexate

Carboxypeptidase G2 (circular permutant CP-N89) K177AMethotrexate experimental SAS data
ROSETTA model
Sample: Carboxypeptidase G2 (circular permutant CP-N89) K177A dimer, 85 kDa Pseudomonas sp. (strain … protein
Methotrexate dimer, 1 kDa
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jun 6
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.5 nm
Dmax 12.7 nm
VolumePorod 104 nm3

SASDLF2 – Pro-CPG2-1 (pro-enzyme design 1 of circular permutant Carboxypeptidase G2-CP-N89-K177A)

Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 experimental SAS data
ROSETTA model
Sample: Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 dimer, 100 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 8
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.6 nm
Dmax 12.4 nm
VolumePorod 125 nm3

SASDLG2 – Pro-CPG2-1 (pro-enzyme design 1 of circular permutant Carboxypeptidase G2-CP-N89-K177A) with Methotrexate

MethotrexatePro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 experimental SAS data
ROSETTA model
Sample: Methotrexate dimer, 1 kDa
Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 dimer, 100 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 8
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.5 nm
Dmax 12.2 nm
VolumePorod 123 nm3

SASDLH2 – Pro-CPG2-2 (pro-enzyme design 2 of circular permutant Carboxypeptidase G2-CP-N89-K177A)

Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 2 experimental SAS data
ROSETTA model
Sample: Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 2 dimer, 100 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 8
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.7 nm
Dmax 12.5 nm
VolumePorod 126 nm3

SASDLJ2 – Pro-CPG2-2 (pro-enzyme design 2 of circular permutant Carboxypeptidase G2-CP-N89-K177A) with Methotrexate

MethotrexatePro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 2 experimental SAS data
ROSETTA model
Sample: Methotrexate dimer, 1 kDa
Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 2 dimer, 100 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 8
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.5 nm
Dmax 12.1 nm
VolumePorod 125 nm3

SASDLK2 – Pro-CPG2-3 (pro-enzyme design 3 of circular permutant Carboxypeptidase G2-CP-N89-K177A)

Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 3 experimental SAS data
ROSETTA model
Sample: Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 3 dimer, 100 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 8
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.7 nm
Dmax 13.0 nm
VolumePorod 127 nm3

SASDLL2 – Pro-CPG2-3 (pro-enzyme design 3 of circular permutant Carboxypeptidase G2-CP-N89-K177A) with Methotrexate

MethotrexatePro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 3 experimental SAS data
ROSETTA model
Sample: Methotrexate dimer, 1 kDa
Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 3 dimer, 100 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 May 8
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.5 nm
Dmax 12.3 nm
VolumePorod 125 nm3

SASDLM2 – Pro-CPG2-1-Disulfide (pro-enzyme design 1 disulfide variant of circular permutant Carboxypeptidase G2-CP-N89-K177A)

Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 Disulfide Variant experimental SAS data
ROSETTA model
Sample: Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 Disulfide Variant dimer, 96 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 6
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.6 nm
Dmax 12.6 nm
VolumePorod 120 nm3

SASDLN2 – Pro-CPG2-1-Disulfide (pro-enzyme design 1 disulfide variant of circular permutant Carboxypeptidase G2-CP-N89-K177A) with Methotrexate

MethotrexatePro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 Disulfide Variant experimental SAS data
ROSETTA model
Sample: Methotrexate dimer, 1 kDa
Pro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 1 Disulfide Variant dimer, 96 kDa Pseudomonas sp. (strain … protein
Buffer: 50 mM Tris, 100 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Dec 6
Massively parallel, computationally guided design of a proenzyme. Proc Natl Acad Sci U S A 119(15):e2116097119 (2022)
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD
RgGuinier 3.5 nm
Dmax 12.3 nm
VolumePorod 125 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

SASDBK5 – Cyclohexanone monooxygenase, K328A

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

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

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

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

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

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

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

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

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

SASDBU5 – Cyclopentadecanone monooxygenase, 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, 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

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