Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase.
Peptidyl-tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a = 47.24 A, b = 63.59 A, and c = 62.57 A. They belong to space group P2(1)2(1)2(1) and diffract to better than 1.2 A resolution. The structure is being solved by multiple isomorphous replacement.
Schmitt
E
E
Laboratoire de Biochimie, Unité de Recherche Associée 1970 du Centre National de la Recherche Scientifique, Palaiseau, France.
Fromant
M
M
Plateau
P
P
Mechulam
Y
Y
Blanquet
S
S
D000433:1-Propanol; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D002460:Cell Line; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology*; D011092:Polyethylene Glycols
D011092:Polyethylene Glycols; D000433:1-Propanol; D002265:Carboxylic Ester Hydrolases; C019674:aminoacyl-tRNA hydrolase