Crystal versus solution structures of thiamine diphosphate-dependent enzymes.

Svergun DI, Petoukhov MV, Koch MH, K├Ânig 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 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.

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