Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli. |
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Authors: | M. Zhou E. D. Wang R. L. Campbell Y. L. Wang S. X. Lin |
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Affiliation: | Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada. |
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Abstract: | Arginyl-tRNA Synthetase, a class I aminoacyl tRNA synthetase playing a crucial role in protein biosynthesis, has been crystallized for the first time. Polyethylene glycol (PEG) was used as a precipitant, and the crystallization proceeded at pH 6.5. These single crystals diffracted to 2.8 A with a rotating anode X-ray source and R-axis IIc image plate detector. They have an orthorhombic space group P2(1)2(1)2 with unit cell parameters of a = 251.51 A, b = 53.12 A, and c = 52.35 A. A complete native data set has been collected at 3.1 A resolution for these crystals. |
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Keywords: | arginyl-tRNA synthetase class I aminoacyl-tRNA synthetase crystallization protein biosynthesis X-ray crystallography |
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