Preliminary crystallographic study of the phenylalanyl-tRNA synthetase from Thermus thermophilus HB8.

Autor: Chernaya MM; Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow., Korolev SV, Reshetnikova LS, Safro MG
Jazyk: angličtina
Zdroj: Journal of molecular biology [J Mol Biol] 1987 Dec 05; Vol. 198 (3), pp. 555-6.
DOI: 10.1016/0022-2836(87)90301-9
Abstrakt: Phenylalanyl-tRNA synthetase (EC 6.1.1.20) from the extreme thermophile Thermus thermophilus HB8 has been isolated and crystallized. The enzyme was found to consist of two types of subunits with molecular masses 38 X 10(3) (alpha) and 94 X 10(3) (beta) and is likely to be a tetrameric protein with a molecular mass of about 260 X 10(3) (alpha 2 beta 2). Crystals of phenylalanyl-tRNA synthetase were grown by the hanging-drop technique at 4 degrees C in the presence of ammonium sulfate. Trigonal crystals, space group P3(1)21, with cell dimensions a = b = 176 A and c = 142 A (1 A = 0.1 nm), are suitable for medium-resolution X-ray analysis.
Databáze: MEDLINE