Crystallization and preliminary crystallographic studies of the W2 domain ofDrosophila melanogastereukaryotic translation initiation factor 5C domain-containing protein

TheDrosophila melanogastereukaryotic translation initiation factor 5C domain-containing protein (ECP) is composed of two independently folded domains which belong to the basic leucine-zipper and W2 domain-containing protein (BZW) family. Based on the sequence similarity between the C-terminal W2 domain of ECP and some eukaryotic translation initiation factors (such as eIF2B∊, eIF4γ, eIF5etc.), ECP has been speculated to participate in the translation initiation process. Structural information on the C-terminal W2 domain of ECP would be helpful in understanding the specific cellular function of this protein. Here, the W2 domain of ECP was expressed and crystallized. Crystals grown by the hanging-drop vapour-diffusion method diffracted to 2.70 Å resolution and belonged to space groupI4, with unit-cell parametersa = b = 81.05,c= 57.44 Å. The Matthews coefficient suggested that there was one molecule per asymmetric unit in the crystal.