Crystals of threonyl-tRNA synthetase from Thermus thermophilus. Preliminary crystallographic data.
Crystals have been obtained of threonyl-tRNA synthetase from the extreme thermophile Thermus thermophilus using sodium formate as a precipitant. The crystals are very stable and diffract to at least 2.4 A. The crystals belong to space group P2(1)2(1)2(1) with cell parameters a = 61.4 A, b = 156.1 A, c = 177.3 A.
Garber
M B
MB
Institute of Protein Research, Academy of Sciences of the U.S.S.R., Puschino, Moscow Region.
Yaremchuk
A D
AD
Tukalo
M A
MA
Egorova
S P
SP
Fomenkova
N P
NP
Nikonov
S V
SV
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification*; D003460:Crystallization; D004795:Enzyme Stability; D011487:Protein Conformation; D013824:Thermus / Q000201:enzymology*; D013914:Threonine-tRNA Ligase / Q000302:isolation & purification*; D014961:X-Ray Diffraction
D000604:Amino Acyl-tRNA Synthetases; D013914:Threonine-tRNA Ligase