Crystals of the phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 complexed with tRNA(Phe).
Phenylalanyl-tRNA synthetase (EC 6.1.1.20) from the extreme thermophile Thermus thermophilus HB8 has been crystallized with its cognate tRNA. Compared with the native crystals, the crystals of the complex are more stable to radiation damage and diffract to 3.0 A resolution. They are of space group P3(2)21, with a = b = 175 A, c = 142.1 A, gamma = 120 degrees, almost identical with the crystal parameters of the native synthetase.
Reshetnikova
L
L
Institute of Molecular Biology, Academy of Science of Russia, Moscow.
Khodyreva
S
S
Lavrik
O
O
Ankilova
V
V
Frolow
F
F
Safro
M
M
D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D010652:Phenylalanine-tRNA Ligase / Q000737:chemistry*; D012360:RNA, Transfer, Phe / Q000737:chemistry*; D016963:Thermus thermophilus / Q000201:enzymology*; D014961:X-Ray Diffraction
D012360:RNA, Transfer, Phe; D010652:Phenylalanine-tRNA Ligase