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Protein Science, Vol 6, Issue 12 2636-2638, Copyright © 1997 by Cold Spring Harbor Laboratory Press

FOR THE RECORD

Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli

M. ZHOU, E. D. WANG, R. L. CAMPBELL, Y. L. WANG and S. X. LIN
Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, 2705 Laurier Boulevard, Quebec, Canada G1V 4G2 Laboratory of Protein Crystals, Inc., Quebec, Canada

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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