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 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.
Charron
Christophe
C
Laboratoire 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.
Manival
Xavier
X
Charpentier
Bruno
B
Branlant
Christiane
C
Aubry
André
A
D019843:Archaeal Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D019641:DNA, Archaeal / Q000737:chemistry / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D016133:Polymerase Chain Reaction; D019711:Pyrococcus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D019843:Archaeal Proteins; D019641:DNA, Archaeal; D011994:Recombinant Proteins; D012261:Ribonucleoproteins