Alignment and merging of electron microscope images of frozen hydrated crystals of the T4 DNA helix destabilizing protein gp32*I.
Alignment and merging of electron microscope images of frozen hydrated crystals of the T4 DNA helix destabilizing protein gp32*I.
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T4 DNA 螺旋不稳定蛋白 gp32*I 的冷冻水合晶体的电子显微镜图像的比对和合并。
DOI：
10.1016/s0006-3495(86)83638-4
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发表时间：
1986
影响因子：
3.4
通讯作者：
Hosoda,J
中科院分区：
文献类型：
--
作者：
Grant,RA;Schmid,MF;Chiu,W;Deatherage,JF;Hosoda,J
低剂量冷冻电子显微镜已被用于记录单链DNA结合蛋白gp32*I的冷冻水合晶体的图像和电子衍射图案。来自13个图像区域的傅立叶变换，对应于大约40，000个单位单元，通过最小相位残差搜索进行对齐，并通过倒易空间中的矢量相加进行合并。将来自所得复合变换的相位与来自电子衍射图案的振幅组合，以8.4 A分辨率重建gp32*I晶体的投影质量密度。
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 gp32*I. 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 gp32*I crystal at 8.4 A resolution.