Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering.

Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM
J Am Chem Soc 132(37):13026-45 (2010 Sep 22)
PMID: 20731394
doi: 10.1021/ja105485b 		Submitted to SASBDB: 2017 May 23
Published in SASBDB:

SASDCN3 – Phosphoenolpyruvate-protein phosphotransferase

Phosphoenolpyruvate-protein phosphotransferase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Phosphoenolpyruvate-protein phosphotransferase dimer, 127 kDa Escherichia coli protein
Buffer: 20mM TRIS buffer, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at 12-ID-C, Advanced Photon Source (APS), Argonne National Laboratory on 2010 Aug 23
RgGuinier 4.1 nm
Dmax 14.8 nm
VolumePorod 189 nm3