Crystallization of the seryl-tRNA synthetase:tRNAS(ser) complex of Escherichia coli.
Crystals of the complex between seryl-tRNA synthetase and tRNA(2ser) from Escherichia coli have been obtained from ammonium sulphate solutions. The crystals are of the 1:2 enzyme:tRNA complex, belong to the space group C222(1), have cell dimensions of a = 128.9 A, b = 164.9 A, c = 127.3 A and diffract anisotropically from 3.5 to 4.5 A. An X-ray diffraction data set to 4 A has been collected. The combination of molecular replacement using the refined structure of the catalytic domain of the native enzyme, data from a heavy atom derivative and solvent flattening was used to produce a map at 4 A resolution. This shows that a tRNA molecule binds across the dimer, the anticodon stem and loop do not contact the protein and the helical arm of the enzyme contacts the T psi C loop and the long extra arm of the tRNA.
Price
S
S
European Molecular Biology Laboratory, Grenoble Outstation, France.
Cusack
S
S
Borel
F
F
Berthet-Colominas
C
C
Leberman
R
R
D003460:Crystallization; D004926:Escherichia coli / Q000737:chemistry*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D012362:RNA, Transfer, Ser / Q000737:chemistry*; D012714:Serine-tRNA Ligase / Q000737:chemistry*; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D012362:RNA, Transfer, Ser; D012714:Serine-tRNA Ligase