A small angle X-ray study of the elongation factor complex Tu . GDP from Escherichia coli.
The protein elongation factor complex Tu. GDP from Escherichia coli was investigated in the presence of 0.01 mM GDP using the small-angle X-ray method. The overall shape and the molecular parameters of the Tu . GDP complex were determined using a least-squares method where the experimental data were used directly without desmearing. The best fit to the experimental data was obtained assuming the molecule to be an ellipsoid of revolution with the semiaxes A = B = 4.08 nm, and C = 1.18nm. Determination of the molecular weight gave the result Mr = 46 000, which corresponds to a water content equal to 26% (by weight).
D001426:Bacterial Proteins; D004926:Escherichia coli; D006153:Guanosine Diphosphate; D008970:Molecular Weight; D010445:Peptide Elongation Factors; D011487:Protein Conformation; D012542:Scattering, Radiation; D014867:Water; D014965:X-Rays
D001426:Bacterial Proteins; D010445:Peptide Elongation Factors; D014867:Water; D006153:Guanosine Diphosphate