Winkler H, Gross H, Schnyder T, Kunath W
Fritz-Haber-Institut der Max-Planck-Gesellschaft, Berlin, Federal Republic of Germany.
J Electron Microsc Tech. 1991 Jun;18(2):135-41. doi: 10.1002/jemt.1060180207.
The structure of mitochondrial creatine kinase is investigated by high-resolution shadowing at very low temperature and conventional negative staining. The electron microscopic images are analyzed with circular harmonic averaging, a method suited for the processing of single molecules. The rotational alignment and averaging is performed with the circular harmonic components, which allows data compression and several steps of noise reduction to be carried out within the averaging procedure. In addition, the symmetry can be deduced. For the mitochondrial creatine kinase, a fourfold symmetry is found that is compatible with the biochemical and biophysical characterization of the molecule.
通过在极低温度下的高分辨率投影和传统负染色法研究线粒体肌酸激酶的结构。利用圆谐波平均法分析电子显微镜图像，该方法适用于单分子的处理。通过圆谐波分量进行旋转对齐和平均，这使得在平均过程中能够进行数据压缩和多个降噪步骤。此外，还可以推导出对称性。对于线粒体肌酸激酶，发现了一种四重对称性，这与该分子的生化和生物物理特征相符。
