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/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 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.
Funder
US Department of Energy (DOE) Office of Science User Facility
US Department of Energy, Office of Science, Office of Workforce Development for Teachers and Scientists
Publisher
International Union of Crystallography (IUCr)
Subject
Instrumentation,Nuclear and High Energy Physics,Radiation
Cited by
5 articles.
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