Crystallization of the seryl-tRNA synthetase-tRNA(Ser) complex from Thermus thermophilus.
The complex between seryl-tRNA synthetase and its cognate tRNA from the extreme thermophile Thermus thermophilus has been crystallized from ammonium sulphate solutions. Two different tetragonal crystal forms have been characterized, both diffracting to about 6 A using synchrotron radiation. One form grows as large bipyramids and has cell dimensions a = b = 127 A, c = 467 A, and the second form occurs as long, thin square prisms with cell dimensions a = b = 101 A, c = 471 A. Analysis of washed and dissolved crystals demonstrates the presence of both protein and tRNA.
Yaremchuk
A D
AD
Institute of Molecular Biology and Genetics, Academy of Sciences, Kiev, U.S.S.R.
Tukalo
M A
MA
Krikliviy
I A
IA
Mel'nik
V N
VN
Berthet-Colominas
C
C
Cusack
S
S
Leberman
R
R
D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D012362:RNA, Transfer, Ser / Q000737:chemistry* / Q000378:metabolism; D012714:Serine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism; D016963:Thermus thermophilus / Q000201:enzymology*; D014961:X-Ray Diffraction
D012362:RNA, Transfer, Ser; D012714:Serine-tRNA Ligase