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 I212121 and P21 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.
|Number of pages||4|
|Journal||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|Publication status||Published - 2009|
All Science Journal Classification (ASJC) codes
- Structural Biology
- Condensed Matter Physics