Direct measurement of Stokes-Einstein diffusion of Cowpea mosaic virus with 19 µs-resolved XPCS.

Brownian motion of Cowpea mosaic virus (CPMV) in water was measured using small-angle X-ray photon correlation spectroscopy (SA-XPCS) at 19.2 µs time resolution. It was found that the decorrelation time τ(Q) = 1/DQ ² up to Q = 0.091 nm ^-1 . The hydrodynamic radius R _H determined from XPCS using Stokes-Einstein diffusion D = kT/(6πηR _H ) is 43% larger than the geometric radius R ₀ determined from SAXS in the 0.007 M K ₃ PO ₄ buffer solution, whereas it is 80% larger for CPMV in 0.5 M NaCl and 104% larger in 0.5 M (NH ₄ ) ₂ SO ₄ , a possible effect of aggregation as well as slight variation of the structures of the capsid resulting from the salt-protein interactions.
(open access.)