Crystallization and preliminary X-ray diffraction analysis of Thermus thermophilus prolyl-tRNA synthetase.
Prolyl-tRNA synthetase from Thermus thermophilus (ProRSTT) was purified to homogeneity using a five-step purification procedure and was crystallized using ethylene glycol as a precipitant. Crystals of ProRSTT belong to the space group P2(1)2(1)2, with unit-cell parameters a = 132, b = 191, c = 125 A, have two homodimers per asymmetric unit and diffract to 2.4 A resolution. A complete native data set to 2.43 A resolution has been collected and a data set from ProRSTT in complex with proline has been collected to 2.9 A resolution.
Yaremchuk
A
A
EMBL Grenoble Outstation, 156X, 38042 Grenoble CEDEX 9, France. yarem@embl-grenoble.fr
Cusack
S
S
Tukalo
M
M
D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000737:chemistry*; D011232:Chemical Precipitation; D003460:Crystallization; D018360:Crystallography, X-Ray; D016963:Thermus thermophilus / Q000201:enzymology*
D001426:Bacterial Proteins; D000604:Amino Acyl-tRNA Synthetases; C100134:prolyl T RNA synthetase