A critical analysis of a paper by Li entitled 'Direct and real-time visualization of the disassembly of a single RecA-DNA-ATPδS complex using AFM imaging in Fluid' is presented. AFM imaging is a powerful tool for visualizing DNA-protein interaction, when one carefully accounts for the influence of tip-sample interactions and tip convolution. The interaction between tip and sample influences the stability of the RecA-DNA filament, causing the great variety observed in dissociation rates. Proteins often lose their relevant biochemical activity in unbuffered deionized conditions. The criticism says that while imaging in buffer, one should try to resemble bulk conditions where proteins and other biological systems are well documented.