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

Abstract:

: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.

journal_name

J Mol Biol

authors

Chernaya MM,Korolev SV,Reshetnikova LS,Safro MG

doi

10.1016/0022-2836(87)90301-9

subject

Has Abstract

pub_date

1987-12-05 00:00:00

pages

555-6

issue

3

eissn

0022-2836

issn

1089-8638

pii

0022-2836(87)90301-9

journal_volume

198

pub_type

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