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. 1997 Dec;6(12):2636-8.
doi: 10.1002/pro.5560061217.

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

M Zhou  1 , E D Wang, R L Campbell, Y L Wang, S X Lin
Affiliations

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

M Zhou et al. Protein Sci. 1997 Dec.

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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