Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase.
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%.
Newberry
K J
KJ
Department of Chemistry and Interdepartmental Program in Biochemistry and Molecular Biology, University of California at Santa Barbara, Santa Barbara CA 93106-9510, USA.
Kohn
J
J
Hou
Y M
YM
Perona
J J
JJ
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
D001426:Bacterial Proteins; D000604:Amino Acyl-tRNA Synthetases; C019975:cysteinyl-tRNA synthetase