The role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.

Yachnin BJ, Lau PCK, Berghuis AM, Biochim Biophys Acta 1864(12):1641-1648 (2016) Europe PMC

SASDBM5 – Cyclohexanone monooxygenase, K328A-W492A

Cyclohexanone monooxygenase
MWI(0) 70 kDa
MWexpected 61 kDa
VPorod 110 nm3
log I(s) 5.16×103 5.16×102 5.16×101 5.16×100
Cyclohexanone monooxygenase small angle scattering data  s, nm-1
ln I(s)
Cyclohexanone monooxygenase Guinier plot ln 5.16×103 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Cyclohexanone monooxygenase Kratky plot 1.104 0 3 sRg
p(r)
Cyclohexanone monooxygenase pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.4 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Cyclohexanone monooxygenase, K328A-W492A in 50 mM Tris, pH 8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a MAR 165 CCD detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.5 and 10 mg/ml were measured at 20°C. Four successive frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Storage temperature = UNKNOWN. X-ray Exposure time = UNKNOWN

Cyclohexanone monooxygenase (CHMO-K328A-W492A)
Mol. type   Protein
Organism   Rhodococcus sp. HI-31
Olig. state   Monomer
Mon. MW   60.6 kDa
 
UniProt   C0STX7
Sequence   FASTA