IYCr crystallization series
The expression, purification, crystallization and preliminary crystallographic analysis of the high-mobility group protein (HMO2) from S. cerevisiae are reported.
crystallization communications
To contribute to the molecular understanding of the function of a tandem-type universal stress protein, UspE from E. coli was overexpressed and crystals of the recombinant protein were obtained using sitting-drop vapour diffusion. A diffraction data set was collected to a resolution of 3.2 Å.