The CP1 domain (the editing domain) of isoleucyl-tRNA synthetase (IleRS) hydrolyzes misactivated Val-AMP in pre-transfer editing and mischarged Val-tRNAIle in post-transfer editing. The CP1 domain of Thermus thermophilus IleRS was expressed in isolation, purified and cocrystallized with Val-AMS (a Val-AMP analogue) and with Val-2AA (a Val-tRNAIle analogue). Two different expression constructs were used for each cocrystallization. The complex crystals with Val-AMS belong to the tetragonal space group P41212, with unit-cell parameters a = b = 102.00, c = 84.88 Å. The asymmetric unit contains two molecules of the CP1 domain, with a corresponding crystal volume per protein weight of 2.7 Å3 Da-1 and a solvent content of 53.5%. The complex crystals with Val-2AA belong to the tetragonal space group P4122, with unit-cell parameters a = b = 72.59, c =83.68 Å. The asymmetric unit contains one molecule of the CP1 domain, with a corresponding crystal volume per protein weight of 2.8 Å3 Da-1 and a solvent content of 55.8%. Data sets diffracting to 1.7 Å resolution were collected from each single crystal at 100 K.
|Original language||English (US)|
|Number of pages||3|
|Journal||Acta Crystallographica Section D: Biological Crystallography|
|State||Published - Oct 1 2004|
ASJC Scopus subject areas
- Structural Biology