Tip49a, a human protein isolated with several chromatin-remodulating complexes, is readily oligomerized in vitro forming polydisperse aggregates of the size of tens and hundreds of nanometers. In this work we show that the non-specific aggregation of the protein can be effectively countered by 0.05–0.10 % concentrations of a detergent Triton-X100. We also show that addition of the detergent destroys aggregates formed already that allows us to isolate oligomeric forms of the protein which may have biological significance. When combined, the results of small angle X-ray scattering and dynamic light scattering experiments suggest that TIP49A aggregation observed in vitro is reversible with the protein oligomerization in two different types of stable filamentous structures.