A standardized load sequence for flight simulation tests on transport aircraft wing structures

Abstract

The morphology of the high molecular weight complex of aminoacyl-tRNA synthetases purified from rabbit reticulocytes has been investigated by electron microscopy. To stabilize it against dissociation, the complex was also studied after chemical crosslinking. Freeze fracture, drying shadowing and negative staining were used. The reticulocyte complex appears as a moderately elongated object with no simple compact shape. Upon rapid drying, the native complex dissociates and shows the presence of approximately 8 globular components, the individual size of which is 80-100 A. The surface of the cross-linked complex shows several distinct globules which appear to extend out of a central core. The irregularly shaped crosslinked complex has a maximal dimension of 350 +/- 50 A. The morphology of the synthetase complex is discussed with respect to some of the properties of this type of multienzymatic system.