Urate Oxidase (Uricase) from Aspergillus flavus

Tsutomu Matsui.

SASDHD2 – Urate Oxidase (Uricase) from Aspergillus flavus, measured by SEC-SAXS

Urate Oxidase (Uricase) from Aspergillus flavus
MWexperimental 141 kDa
MWexpected 137 kDa
VPorod 225 nm3
log I(s) 8.40×10-2 8.40×10-3 8.40×10-4 8.40×10-5
Urate Oxidase (Uricase) from Aspergillus flavus small angle scattering data  s, nm-1
ln I(s)
Urate Oxidase (Uricase) from Aspergillus flavus Guinier plot ln 8.40×10-2 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Urate Oxidase (Uricase) from Aspergillus flavus Kratky plot 1.104 0 √3 sRg
p(r)
Urate Oxidase (Uricase) from Aspergillus flavus pair distance distribution function Rg: 3.2 nm 0 Dmax: 9.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Urate Oxidase (Uricase) from Aspergillus flavus CORAL model
log I(s)
 s, nm-1
Urate Oxidase (Uricase) from Aspergillus flavus DAMMIN model
Synchrotron SAXS data from solutions of Uricase in 20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT, pH 8, were collected on the BL4-2 beam line at the Stanford Synchrotron Radiation Lightsource (SSRL; Menlo Park, CA, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 1.7 m and at a wavelength of λ = 0.112709 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50 μl sample at 5 mg/ml was injected at a 0.05 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 23°C. 500 successive 1 second frames were collected throughout the entire SEC run. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank (from the SEC column eluate) were subtracted from the appropriate sample peak frames.

Urate Oxidase (Uricase) from Aspergillus flavus (Urate Oxidase)
Mol. type   Protein
Organism   Aspergillus flavus
Olig. state   Tetramer
Mon. MW   34.2 kDa
 
UniProt   Q00511 (1-302)
Sequence   FASTA
 
PDB ID   4POE