title: Overexpression, purification and crystallization of tyrosyl-tRNA synthetase from the hyperthermophilic archaeon Aeropyrum pernix K1.
abstract: Hyperthermophilic archaeal tyrosyl-tRNA synthetase from Aeropyrum pernix K1 was cloned and overexpressed in Escherichia coli. The expressed protein was purified by Cibacron Blue affinity chromatography following heat treatment at 363 K. Crystals suitable for X-ray diffraction studies were obtained under optimized crystallization conditions in the presence of 1.5 M ammonium sulfate using the hanging-drop vapour-diffusion method. The crystals belonged to the tetragonal space group P4(3)2(1)2, with unit-cell parameters a = b = 66.1, c = 196.2 A, and diffracted to beyond 2.15 A resolution at 100 K.
authors.affiliation: Department of Material and Biological Chemistry, Faculty of Science, Yamagata University, Yamagata 990-8560, Japan.
authors.forename: Jun
authors.initials: J
authors.lastname: Iwaki
authors.forename: Ryuichiro
authors.initials: R
authors.lastname: Suzuki
authors.forename: Zui
authors.initials: Z
authors.lastname: Fujimoto
authors.forename: Mitsuru
authors.initials: M
authors.lastname: Momma
authors.forename: Atsushi
authors.initials: A
authors.lastname: Kuno
authors.forename: Tsunemi
authors.initials: T
authors.lastname: Hasegawa
mesh_terms: D041522:Aeropyrum / Q000378:metabolism*; D000645:Ammonium Sulfate / Q000494:pharmacology; D019843:Archaeal Proteins / Q000737:chemistry*; D002845:Chromatography; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000378:metabolism; D006358:Hot Temperature; D013696:Temperature; D014448:Tyrosine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
chemical_list: D019843:Archaeal Proteins; D014448:Tyrosine-tRNA Ligase; D000645:Ammonium Sulfate