Purification, crystallization and preliminary X-ray diffraction data of L7Ae sRNP core protein from Pyrococcus abyssii

The L7Ae sRNP core protein from Pyrococcus abyssii was crystallized using the sitting- drop vapour- diffusion method. Crystals were obtained in the presence of MgCl2, PEG 2000 MME and acetate buffer at pH 4.0. A native data set has been collected at 2.9 Angstrom resolution using a rotating- anode generator at room temperature. Crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 70.7, b = 112.9, c = 34.8 Angstrom. There are two monomers of MW 14 200 Da per asymmetric unit and the packing density V-M is 2.45 Angstrom(3) Da(-1). A molecular- replacement analysis gave solutions for the rotation and translation functions.