Open AccessCrystallization and preliminary X‐ray diffraction analysis of the tRNA‐modification enzyme GidA from Aquifex aeolicus
Author(s) -
Osawa Takuo,
Inanaga Hideko,
Numata Tomoyuki
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109013591
Subject(s) - aquifex aeolicus , diffraction , transfer rna , crystallization , x ray crystallography , crystallography , materials science , chemistry , physics , rna , optics , biochemistry , gene , organic chemistry , escherichia coli
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 Å resolution, respectively, using synchrotron radiation at the Photon Factory. These crystals belonged to space groups I 2 1 2 1 2 1 and P 2 1 with unit‐cell parameters a = 101.6, b = 213.3, c = 231.7 Å and a = 119.4, b = 98.0, c = 129.6 Å, β = 90.002°, respectively. The asymmetric units of these crystals are expected to contain two and four molecules, respectively.