Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.

Korasick DA, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ, FEBS J 284(18):3029-3049 (2017) Europe PMC

SASDC24 – Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) R51E mutant 4.7 mg/mL

Proline dehydrogenase
MWexperimental 216 kDa
MWexpected 215 kDa
VPorod 283 nm3
log I(s) 2.32×102 2.32×101 2.32×100 2.32×10-1
Proline dehydrogenase small angle scattering data  s, nm-1
ln I(s)
Proline dehydrogenase Guinier plot ln 2.32×102 Rg: 4.5 nm 0 (4.5 nm)-2 s2
(sRg)2I(s)/I(0)
Proline dehydrogenase Kratky plot 1.104 0 √3 sRg
p(r)
Proline dehydrogenase pair distance distribution function Rg: 4.5 nm 0 Dmax: 13.9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) R51E mutant in 50 mM Tris, 50 mM NaCl, 0.5 mM Tris(2-carboxyethyl)phosphine, and 5% (v/v) glycerol, pH 7.8 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a Pilatus3 X 2M detector (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 4.7 mg/ml was measured. The data were normalized to the intensity of the transmitted beam and radially averaged. The radially averaged scattering of the solvent-blank was subtracted. X-ray wavelength, unknown; Exposure time, unknown; Sample-To-Detector distance, unknown.

Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Proline dehydrogenase (BjPutA R51E)
Mol. type   Protein
Organism   Bradyrhizobium diazoefficiens
Olig. state   Dimer
Mon. MW   107.5 kDa
 
UniProt   Q89E26
Sequence   FASTA