TY - JOUR
T1 - Crystallization of a small fragment of an aminoacyl tRNA synthetase
AU - Frederick, Christin A.
AU - Wang, Andrew H.J.
AU - Rich, Alexander
AU - Regan, Lynne
AU - Schimmel, Paul
N1 - Funding Information:
This work was supported GM37641 from the National
PY - 1988/9/20
Y1 - 1988/9/20
N2 - Single crystals of an amino-terminal fragment of Escherichia coli alanine tRNA synthetase have been prepared by the vapor diffusion method. The fragment extends to amino acid residue 368 and catalyzes the synthesis of alanyl adenylate. The crystals grow in the presence of alanine as rhombic plates in space group P212121 and with unit cell dimensions of a = 67.9 A ̊, b = 98.5 A ̊ and c = 123.6 A ̊ (1 Å = 0.1 nm). They diffract to better than 3 Å resolution.
AB - Single crystals of an amino-terminal fragment of Escherichia coli alanine tRNA synthetase have been prepared by the vapor diffusion method. The fragment extends to amino acid residue 368 and catalyzes the synthesis of alanyl adenylate. The crystals grow in the presence of alanine as rhombic plates in space group P212121 and with unit cell dimensions of a = 67.9 A ̊, b = 98.5 A ̊ and c = 123.6 A ̊ (1 Å = 0.1 nm). They diffract to better than 3 Å resolution.
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U2 - 10.1016/0022-2836(88)90019-8
DO - 10.1016/0022-2836(88)90019-8
M3 - Article
C2 - 3058989
AN - SCOPUS:0024293190
SN - 0022-2836
VL - 203
SP - 521
EP - 522
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 2
ER -