The universal stress proteins (Usp) homolog proteins are among the most highly induced genes when the bacteria are subjected to several stress conditions such as heat shock, nutrient starvation, the presence of oxidants, or other stress agents.Escherichia coli has five small Usps and one tandem-type Usp.UspE (or YdaA) belongs to the tandem-type Usp and consists of two Usp-domains in a tandem manner.To date, the structure of the UspE remains to be elucidated.To contribute to a molecular understanding of the tandem-type UspE function, we overexpressed the UspE from E.coli and purified the recombinant protein using Ni-NTA affinity, Q anion-exchange and gelfiltration chromatography.The crystals of UspE were obtained by hanging-drop vapour diffusion.A diffraction data set was collected to a resolution of 3.2 (A) with flash-cooled crystals.The crystals belonged to the tetragonal space group I4122 or I4322 with unitcell parameters a =b =121.1 and c =241.7 (A).