The structural analysis of dephosphocholinase Legionella pneumophila Lem3

Wenhua Zhang.

SASDCN8 – SAXS data of Legionella pneumophila phosphocholine hydrolase Lem3(19-570)

Phosphocholine hydrolase Lem3
MWexperimental 67 kDa
MWexpected 63 kDa
VPorod 95 nm3
log I(s) 5.14×10-2 5.14×10-3 5.14×10-4 5.14×10-5
Phosphocholine hydrolase Lem3 small angle scattering data  s, nm-1
ln I(s)
Phosphocholine hydrolase Lem3 Guinier plot ln 5.14×10-2 Rg: 3.5 nm 0 (3.5 nm)-2 s2
(sRg)2I(s)/I(0)
Phosphocholine hydrolase Lem3 Kratky plot 1.104 0 3 sRg
p(r)
Phosphocholine hydrolase Lem3 pair distance distribution function Rg: 3.5 nm 0 Dmax: 12.2 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of SAXS data of Legionella pneumophila phosphocholine hydrolase (19-570) in 300 mM NaCl, 2 mM 2-mercaptoethanol and 30 mM Tris-HCl, pH 7.5 were collected on the SWING beam line at the SOLEIL storage ring (Saint-Aubin, France) using a CCD AVIEX detector at a sample-detector distance of 1.2 m and at a wavelength of λ = 0.102 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Solute concentrations ranging between 4 and 6 mg/ml were measured at 15°C for a total exposure time of 1.5 s. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the data were scaled for protein concentration.

Storage temperature = UNKNOWN

Phosphocholine hydrolase Lem3 (Lem3)
Mol. type   Protein
Organism   Legionella pneumophila subsp. pneumophila
Olig. state   Monomer
Mon. MW   63.4 kDa
 
UniProt   Q5ZXN5 (19-570)
Sequence   FASTA