title: Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase.
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%.
authors.affiliation: Department of Chemistry and Interdepartmental Program in Biochemistry and Molecular Biology, University of California at Santa Barbara, Santa Barbara CA 93106-9510, USA.
authors.forename: K J
authors.initials: KJ
authors.lastname: Newberry
authors.forename: J
authors.initials: J
authors.lastname: Kohn
authors.forename: Y M
authors.initials: YM
authors.lastname: Hou
authors.forename: J J
authors.initials: JJ
authors.lastname: Perona
mesh_terms: D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D011487:Protein Conformation
chemical_list: D001426:Bacterial Proteins; D000604:Amino Acyl-tRNA Synthetases; C019975:cysteinyl-tRNA synthetase