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Purification, crystallization and preliminary X-ray diffraction data of L7Ae sRNP core protein from Pyrococcus
Christophe Charron1, Xavier Manival, Bruno Charpentier
1Laboratoire de Cristallographie et Modélisation des Matériaux Minéraux et Biologiques, UMR 7036 CNRS-UHP, Groupe Biocristallographie, Faculté des Sciences et Techniques, BP 239, 54506 Vandoeuvre-lès-Nancy, France.
Abstract:
The L7Ae sRNP core protein from Pyrococcus abyssii was crystallized using the sitting-drop vapour-diffusion method. Crystals were obtained in the presence of MgCl(2), PEG 2000 MME and acetate buffer at pH 4.0. A native data set has been collected at 2.9 A 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 A. There are two monomers of MW 14 200 Da per asymmetric unit and the packing density V(M) is 2.45 A(3) Da(-1). A molecular-replacement analysis gave solutions for the rotation and translation functions.