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The crystal structure of the single-stranded DNA-binding protein from Thermus aquaticus has been solved and refined at 1.85 Å resolution. Two monomers, each encompassing two oligonucleotide/oligosaccharide-binding (OB) domains and a number of flexible β-hairpin loops, form an oligomer of approximate D2 symmetry typical of bacterial SSBs. Comparison with other SSB structures confirms considerable variability in the mode of oligomerization and aggregation of SSB oligomers.