Crystallization and preliminary crystallographic studies of a ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus celer

Ribosomal protein L30e from the hyperthermophilic archaeon Thermococcus cel er is a good model for the study of the thermostability of proteins. It has been overexpressed, purified and crystallized using the hanging-drop vapou r-diffusion method using PEG 8000 as precipitant at 290 K. The crystal belo ngs to the hexagonal space group P6(1)/P6(5), with unit-cell parameters a = b = 48.32, c = 86.42 Angstrom. The asymmetric unit contains a single molec ule of L30e, with a corresponding crystal volume per protein mass (V-M) of 2.68 Angstrom (3) Da(-1) and a solvent content of 54%. A complete data set diffracting to 1.96 Angstrom resolution was collected from a single crystal at 100 K.