Abstract
Conditions have been established for the crystallization of tyrosyl-transfer RNA synthetase from Bacillus stearothermophilus at room temperature. The crystals are extremely well-ordered, exhibiting diffraction spots out to at least 2.7 Å, and can be grown to a convenient size for X-ray crystallographic analysis. The crystals are trigonal with a space group P3 121, the unit cell having dimensions of a = 64.4 A ̊ and c = 238 A ̊ ; the crystallographic asymmetric unit is probably one subunit of the dimeric (2 × 45,000, mol. wt) enzyme. The enzyme crystals are extremely stable and exhibit good resistance to radiation damage. This amino-acyl-tRNA synthetase appears to be amenable to complete structure determination by X-ray crystallography.
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