Crystallization of Bacillus subtilis tryptophanyl-tRNA synthetase.
Tryptophanyl-tRNA synthetase from Bacillus subtilis was overexpressed in Escherichia coli and was purified using column chromatography on DEAE-Sephacel and hydroxyapatite columns. Single crystals of the synthetase were grown by vapor diffusion at 4 degrees C from pH 5.5 solutions of polyethylene glycol 8000 containing magnesium ATP and L-tryptophan. The crystals diffracted to about 4.0 A resolution at -150 degrees C and appeared to belong to the orthorhombic space group P2(1)2(1)2 with unit cell dimensions: a = 143.6 A, b = 111.6 A, c = 50.6 A with one dimer in the asymmetric unit.
Ala
P
P
Department of Biochemistry, McMaster University, Hamilton, Ontario, Canada.
Xue
H
H
Leung
L
L
Xue
Y Q
YQ
Wong
J T
JT
Yang
D S
DS
D001412:Bacillus subtilis / Q000201:enzymology*; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli; D011994:Recombinant Proteins / Q000737:chemistry; D014369:Tryptophan-tRNA Ligase / Q000737:chemistry*; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D014369:Tryptophan-tRNA Ligase