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Abstract
That ribosomal subunits can exist in active and inactive functional states, and that
subunits in the two states are interconvertible, has been known for some time (see
Zamir et al., 1974). The magnitude of the conformational perturbation accompanying
this functional transformation, however, was not known. In the present study 30 S
and 50 S subunits in the two functional states have been compared by small-angle X-ray
scattering. The results indicate that the structural differences between active and
inactive subunits are small, at the limit of resolution of this technique. Model studies
show that the data imply conformational differences at or below the limit of resolution
of other physical methods now in use to examine the detailed structure of these particles.