Fig. 1.

Measurements of A3G oligomerization using AFM imaging. a The number of monomers per A3G cluster formed on ssDNA are plotted in a histogram. FW A3G (NTD mutant) is mostly bound to the ssDNA in a monomeric form. For IY and RDDQ A3G (CTD mutants) the most common state is a dimer. WT A3G is more likely to form tetramers and larger oligomers as compared to the mutants. b Comparison of average cluster size for WT and mutant A3G. Mutating the CTD moderately reduces oligomerization whereas mutating the NTD disrupts oligomerization to an even greater degree. Error bars are SE based on the size of individual protein clusters formed on at least seven DNA constructs per A3G variant