PMID:9416614
| Citation |
Zhou, M, Wang, ED, Campbell, RL, Wang, YL and Lin, SX (1997) Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli. Protein Sci. 6:2636-8 |
|---|---|
| Abstract |
Arginyl-tRNA Synthetase, a class I aminoacyl tRNA synthetase playing a crucial role in protein biosynthesis, has been crystallized for the first time. Polyethylene glycol (PEG) was used as a precipitant, and the crystallization proceeded at pH 6.5. These single crystals diffracted to 2.8 A with a rotating anode X-ray source and R-axis IIc image plate detector. They have an orthorhombic space group P2(1)2(1)2 with unit cell parameters of a = 251.51 A, b = 53.12 A, and c = 52.35 A. A complete native data set has been collected at 3.1 A resolution for these crystals. |
| Links |
PubMed PMC2143609 Online version:10.1002/pro.5560061217 |
| Keywords |
Arginine-tRNA Ligase/chemistry; Chemical Precipitation; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Hydrogen-Ion Concentration; Molecular Weight; Polyethylene Glycols |
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