Preliminary crystallographic study of the phenylalanyl-tRNA synthetase from Thermus thermophilus HB8.
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.
Chernaya
M M
MM
Institute of Molecular Biology, Academy of Sciences of the USSR, Moscow.
Korolev
S V
SV
Reshetnikova
L S
LS
Safro
M G
MG
D000604:Amino Acyl-tRNA Synthetases; D012345:RNA, Transfer, Amino Acid-Specific; D012360:RNA, Transfer, Phe; D013824:Thermus / Q000201:enzymology*; D014961:X-Ray Diffraction
D012345:RNA, Transfer, Amino Acid-Specific; D012360:RNA, Transfer, Phe; D000604:Amino Acyl-tRNA Synthetases