Open AccessCrystallization of tRNA Leu -Synthetase from Baker's Yeast
Author(s) -
Jack G. Chirikjian,
H.T. Wright,
Jacques R. Fresco
Publication year - 1972
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.69.6.1638
Subject(s) - orthorhombic crystal system , ammonium sulfate , crystallization , transfer rna , crystallography , yeast , protein subunit , enzyme , resolution (logic) , crystal structure , chemistry , stereochemistry , biochemistry , rna , organic chemistry , artificial intelligence , computer science , gene
tRNALeu -Synthetase from baker's yeast has been crystallized from ammonium sulfate solution. The crystals are of orthorhombic symmetry, falling into space group [unk] or [unk] witha = 75.5 Å,b = 110.7 Å, andc = 124.0 Å. This unit cell contains four molecules of the native (dimeric) enzyme, with eight asymmetric units, each corresponding to the enzyme subunit. Diffraction patterns obtained for the three major projections contain reflections to spacings of less than 3.5 Å, indicating that this crystal form is amenable to structure analysis to atomic resolution.