Shelley K, McPherson A
J Microsc. 1981 Feb;121(Pt 2):201-10. doi: 10.1111/j.1365-2818.1981.tb01213.x.
Microcrystals of B. subtilis alpha-amylase have been negatively stained and examined by electron microscopy. The micrographs were then subjected to spatial filtering and averaging using a Fourier transform procedure programmed for a mini computer. From these 'enhanced' images refined crystallographic parameters were obtained and a model for the packing of the asymmetric units within the crystal was derived. In addition, these parameters obtained from electron microscopy are compared with those derived from limited X-ray diffraction data on macrocrystals of the same form.
