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

Abstract

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/DQ2 up to Q = 0.091 nm−1. The hydrodynamic radius RH determined from XPCS using Stokes–Einstein diffusion D = kT/(6πηRH) is 43% larger than the geometric radius R0 determined from SAXS in the 0.007 M K3PO4 buffer solution, whereas it is 80% larger for CPMV in 0.5 M NaCl and 104% larger in 0.5 M (NH4)2SO4, a possible effect of aggregation as well as slight variation of the structures of the capsid resulting from the salt–protein interactions.

Keywords

• xpcs
• saxs
• biomolecules
• virus-like particles (vlps)
• high-speed x-ray detectors