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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Archaeal Proteins / chemistry*
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Archaeal Proteins / genetics
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Archaeal Proteins / isolation & purification
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Crystallization
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Crystallography, X-Ray
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DNA, Archaeal / chemistry
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DNA, Archaeal / genetics
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Escherichia coli / genetics
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Polymerase Chain Reaction
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Pyrococcus / chemistry*
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Pyrococcus / genetics
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Pyrococcus / metabolism
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Ribonucleoproteins / chemistry*
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Ribonucleoproteins / genetics
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Ribonucleoproteins / isolation & purification
Substances
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Archaeal Proteins
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DNA, Archaeal
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Recombinant Proteins
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Ribonucleoproteins