Publication Abstract from PubMed
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.
Purification, crystallization and preliminary X-ray diffraction data of L7Ae sRNP core protein from Pyrococcus abyssii.,Charron C, Manival X, Charpentier B, Branlant C, Aubry A Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):122-4. Epub 2003, Dec 18. PMID:14684904[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
