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Crystallization and preliminary X-ray diffraction analysis of the tRNA-modification enzyme GidA from Aquifex aeolicus.

Authors
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
1744-3091
Publisher
International Union of Crystallography
Publication Date
Volume
65
Issue
Pt 5
Pages
508–511
Identifiers
DOI: 10.1107/S1744309109013591
PMID: 19407389
Source
Medline

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.

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