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. Author manuscript; available in PMC: 2019 Oct 2.
Published in final edited form as: Structure. 2018 Aug 9;26(10):1314–1326.e4. doi: 10.1016/j.str.2018.06.012

Figure 6. Sedimentation Velocity Analysis of rHBcAg Alone and in Complex with scFv e13.

Figure 6.

Raw absorbance scans of (A) rHBcAg at pH 9.5, (B) rHBcAg at pH 7.5 and 250 mM NaCl, (C) rHBcAg-scFv e13 at pH 9.5, and (D) rHBcAg-scFv e13 at pH 7.5 and 250 mM NaCl. All analyses were performed at 40,000 rpm except for rHBcAg at pH 7.5 and 250 mM NaCl, which was performed at 25,000 rpm. The red arrow indicates the direction of sedimentation from top (meniscus) to bottom of the analytical cells. At pH 9.5 the rHBcAg is dimeric with a sedimentation coefficient (s) of ~ 2.4 whereas at pH 7.5 and 250 mM NaCl (assembly conditions) the protein has s values of 42 – 45, corresponding to capsids [45]. Approximately 1015% unassembled protein is also present. The rHBcAg-scFv e13 complex, previously resolved by gel filtration at pH 9.5, has an s value of 4.3. The same complex under assembly conditions also has an s value of 4.3. See also Figure S7 and Figure S8.