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Protein homo-oligomerization is a very common phenomenon, and approximately half of proteins form homo-oligomeric assemblies composed of identical subunits. The vast majority of such assemblies possess internal symmetry which can be either exploited to help or poses challenges during structure determination. Moreover, aspects of symmetry are critical in the modeling of protein homo-oligomers either by docking or by homology-based approaches. Here, we first provide a brief overview of the naturedoi:10.3390/ijms22169081 pmid:34445785 pmcid:PMC8396596 fatcat:yd4qi4zhlbbapfl5v242ml2axy