Grant R A, Schmid M F, Chiu W, Deatherage J F, Hosoda J
Biophys J. 1986 Jan;49(1):251-8. doi: 10.1016/S0006-3495(86)83638-4.
Low dose cryoelectron microscopy has been used to record images and electron diffraction patterns of frozen hydrated crystals of the single-stranded DNA binding protein gp32I. Fourier transforms from 13 image areas, corresponding to approximately 40,000 unit cells, were aligned by a minimal phase residual search and merged by vector addition in reciprocal space. Phases from the resulting composite transform were combined with amplitudes from electron diffraction patterns to reconstruct the projected mass density of the gp32I crystal at 8.4 A resolution.
低剂量冷冻电子显微镜已被用于记录单链DNA结合蛋白gp32I的冷冻水合晶体的图像和电子衍射图案。通过最小相位残差搜索对来自13个图像区域（对应于约40,000个晶胞）的傅里叶变换进行对齐，并在倒易空间中通过矢量相加进行合并。将所得复合变换的相位与电子衍射图案的振幅相结合，以8.4埃的分辨率重建gp32I晶体的投影质量密度。
