Crystallization and preliminary X-ray analysis of the archaeosine tRNA-guanine transglycosylase from Pyrococcus horikoshii.
The archaeosine tRNA-guanine transglycosylase from the hyperthermophilic archaeon Pyrococcus horikoshii was crystallized and preliminary X-ray characterization was performed. Single crystals were grown by the hanging-drop vapour-diffusion method, using sodium/potassium phosphate and sodium acetate as precipitants. The space group is P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 99.28 (14), c = 363.74 (56) A. The cryocooled crystals diffracted X-rays beyond 2.2 A resolution using synchrotron radiation from station BL44XU at SPring-8 (Harima). Selenomethionine-substituted protein crystals were prepared in order to solve the structure by the MAD phasing method.
Ishitani
R
R
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
Nureki
O
O
Kijimoto
T
T
Watanabe
M
M
Kondo
H
H
Nameki
N
N
Okada
N
N
Nishimura
S
S
Yokoyama
S
S
D003460:Crystallization; D018360:Crystallography, X-Ray; D010430:Pentosyltransferases / Q000737:chemistry*; D011487:Protein Conformation; D019711:Pyrococcus / Q000201:enzymology*; D012645:Selenomethionine / Q000737:chemistry
D012645:Selenomethionine; D010430:Pentosyltransferases; C020837:queuine tRNA-ribosyltransferase