Crystallization and preliminary X-ray crystallographic studies of the small form of glucose-inhibited division protein A fromThermus thermophilusHB8
- 25 February 2004
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 60 (3) , 515-517
- https://doi.org/10.1107/s0907444904000721
Abstract
Glucose-inhibited division protein A (GidA) acts in tRNA modification. It has been suggested that GidA is involved in the biosynthesis of the hypermodified nucleotide 5-methylaminomethyl-2-thiouridine in the wobble position of bacterial tRNAs, which stabilizes codon-anticodon interactions. Thermus thermophilus HB8 has a putative small gidA gene in addition to the normal gidA gene. The crystallization and preliminary X-ray crystallographic studies of the product of this small gidA gene (GidA(small)) are reported here. The crystals belong to space group P3(1)21 or P3(2)21, with unit-cell parameters a = b = 78.51, c = 66.10 A and one monomer per asymmetric unit. The crystals were found to diffract X-rays to beyond 1.65 A resolution.Keywords
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