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

J Synchrotron Radiat. 2022 Nov 1;29(Pt 6):1429-1435. doi: 10.1107/S1600577522008402. Epub 2022 Oct 10.

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: SAXS; XPCS; biomolecules; high-speed X-ray detectors; virus-like particles (VLPs).

MeSH terms

  • Capsid
  • Comovirus* / chemistry
  • Scattering, Small Angle
  • X-Ray Diffraction

Grants and funding

This research was performed at beamline 8-ID-I of the Advanced Photon Source, a US Department of Energy (DOE) Office of Science User Facility operated for the DOE Office of Science by ANL (contract No. DE-AC02-06CH11357). This work was supported in part by the US Department of Energy, Office of Science, Office of Workforce Development for Teachers and Scientists (WDTS) under the Science Undergraduate Laboratory Internships Program (SULI).