Crystal structures and small-angle x-ray scattering analysis of UDP-galactopyranose mutase from the pathogenic fungus Aspergillus fumigatus.

Dhatwalia R, Singh H, Oppenheimer M, Karr DB, Nix JC, Sobrado P, Tanner JJ, J Biol Chem 287(12):9041-51 (2012) Europe PMC

SASDDK2 – Aspergillus fumigatus UDP galactopyranose mutase

Aspergillus fumigatus UDP galactopyranose mutase

MW^experimental	228	kDa
MW^expected	228	kDa
V^Porod	308	nm³

log I(s) 8.92×10² 8.92×10¹ 8.92×10⁰ 8.92×10^-1

Aspergillus fumigatus UDP galactopyranose mutase small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

Aspergillus fumigatus UDP galactopyranose mutase Guinier plot

ln 8.93×10² R_g: 4.7 nm 0 (4.7 nm)^-2 s²

(sR_g)²I(s)/I(0)

Aspergillus fumigatus UDP galactopyranose mutase Kratky plot

1.104 0 √3 sR_g

p(r)	R_g: 4.8 nm 0 D_max: 14.7 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.5

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0
2.133

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Aspergillus fumigatus UDP galactopyranose mutase MES-FOXS model

Synchrotron SAXS data from solutions of Aspergillus fumigatus UDP galactopyranose mutase in 20 mM HEPES, 45 mM NaCl, 0.5 mM Tris(hydroxypropyl)phosphine, pH 7.5, were collected on the 12.3.1 SIBYLS beam line at the Advanced Light Source storage ring (ALS; Berkeley, CA, USA) using a MAR 165 CCD detector at a wavelength of λ = 0.1127 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 9.00 mg/ml was measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

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

Aspergillus fumigatus UDP galactopyranose mutase
Mol. type		Protein
Olig. state		Tetramer
Mon. MW		57.1 kDa
Sequence		FASTA