PMID:10216301

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Citation

Newberry, KJ, Kohn, J, Hou, YM and Perona, JJ (1999) Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase. Acta Crystallogr. D Biol. Crystallogr. 55:1046-7

Abstract

Crystals of the 52 kDa monomeric Escherichia coli cysteinyl-tRNA synthetase complexed with ATP and cysteine have been grown by hanging-drop vapor diffusion from solutions containing ammonium sulfate as the precipitating agent. The crystals form long hexagonal rods in the space group P321 with unit-cell dimensions a = b = 82.3, c = 168.9 A. There is one enzyme molecule in the asymmetric unit. A complete native data set has been collected from a rotating-anode source to a resolution of 2.7 A at 103 K, with an Rmerge of 6.7%.

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Keywords

Amino Acyl-tRNA Synthetases/chemistry; Amino Acyl-tRNA Synthetases/isolation & purification; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Protein Conformation

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