Crystal versus solution structures of thiamine diphosphate-dependent enzymes.

Svergun DI, Petoukhov MV, Koch MH, König S, J Biol Chem 275(1):297-302 (2000) Europe PMC

SASDAX2 – Pyruvate decarboxylase (PDC) from Z. mobilis

Pyruvate decarboxylase
MWexperimental 247 kDa
MWexpected 244 kDa
log I(s) 1.02×101 1.02×100 1.02×10-1 1.02×10-2
Pyruvate decarboxylase small angle scattering data  s, nm-1
ln I(s)
Pyruvate decarboxylase Guinier plot ln 1.02×101 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Pyruvate decarboxylase Kratky plot 1.104 0 √3 sRg
p(r)
Pyruvate decarboxylase pair distance distribution function Rg: 3.8 nm 0 Dmax: 11 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Pyruvate decarboxylase CRYSOL model
Synchrotron SAXS data from solutions of Pyruvate decarboxylase (PDC) from Z. mobilis in 100 mM Sodium Citrate, 17% Glycerol, 22.5% PEG 1500, pH 6 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a 1D Gas detector detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). . 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.

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

Tags: X33
Pyruvate decarboxylase (ZmPDC)
Mol. type   Protein
Organism   Zymomonas mobilis
Olig. state   Tetramer
Mon. MW   60.9 kDa
 
UniProt   P06672
Sequence   FASTA