Skip to main content
. Author manuscript; available in PMC: 2014 Jan 8.
Published in final edited form as: Structure. 2012 Dec 6;21(1):133–142. doi: 10.1016/j.str.2012.10.017

Figure 3. Centrifugation and electron microscopy experiments on HBeAg in reduced and oxidized forms.

Figure 3

(A, B) Sedimentation velocity analyses performed on (A) oxidized and (B) reduced HBeAg using a Beckman Optima XL-I analytical ultracentrifuge, absorption optics, an An-60 Ti rotor, and standard double-sector centerpiece cells. Measurements at 20 °C were taken at 45,000 rpm for 3 hours with data collection at 10 minute intervals. The profiles show protein absorbance at 280 nm as a function of radial distance.

(C, D) Negative-staining EM of assembly products of (C) oxidized and (D) reduced HBeAg. Both samples, in PBS +/− DTT, were buffer-exchanged into TBS to avoid precipitation. Both images are at the same magnification; capsids are ~32 nm in diameter.