Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli.
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.
Zhou
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Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada.
Wang
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Campbell
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RL
Wang
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Lin
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SX
D001126:Arginine-tRNA Ligase / Q000737:chemistry*; D011232:Chemical Precipitation; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011092:Polyethylene Glycols
D011092:Polyethylene Glycols; D001126:Arginine-tRNA Ligase