title: Crystallization and preliminary X-ray diffraction analysis of the tRNA-modification enzyme GidA from Aquifex aeolicus.
abstract: The 5-carboxymethylaminomethyl modification of uridine at the first position of the tRNA anticodon is crucial for accurate protein synthesis by stabilizing the correct codon-anticodon pairing on the ribosome. Two conserved enzymes, GidA and MnmE, are involved in this modification process. Aquifex aeolicus GidA was crystallized in two different crystal forms: forms I and II. These crystals diffracted to 3.2 and 2.3 A resolution, respectively, using synchrotron radiation at the Photon Factory. These crystals belonged to space groups I2(1)2(1)2(1) and P2(1) with unit-cell parameters a = 101.6, b = 213.3, c = 231.7 A and a = 119.4, b = 98.0, c = 129.6 A, beta = 90.002 degrees , respectively. The asymmetric units of these crystals are expected to contain two and four molecules, respectively.
authors.affiliation: Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Higashi, Tsukuba-shi, Ibaraki, Japan.
authors.forename: Takuo
authors.initials: T
authors.lastname: Osawa
authors.forename: Hideko
authors.initials: H
authors.lastname: Inanaga
authors.forename: Tomoyuki
authors.initials: T
authors.lastname: Numata
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D012343:RNA, Transfer / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; C108512:glucose-inhibited division protein A, bacteria; D012343:RNA, Transfer