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In this theoretical study, the author firstly discusses the wave interferenceof Bragg diffraction inside 3D crystal, followed by quantum mechanicalinterpretation on the diffraction process, and proves that the interferencefringe between Bragg diffraction and the incident beam is identical to thelattice plane. By introducing the beam expander concept, we may explain theimage projection mechanism of Bragg diffractions propagating through TEM:Transmission Electron Microscope. In practice, we will take projection imagesat zone axes, because of its symmetric high-density diffractions associatedwith flat Ewald sphere and minimum overlap with the neighboring molecules. Byprecessing the illuminating beam around the zone axis, and introducing annularobjective aperture, we select only the kinematic Bragg diffractions whichcorrectly contribute to the real image reconstruction on the 2D electrondetector. The outcome should be a positive contrast, clean image with nodynamical diffractions nor Moir\'e patterns. Importantly, the image should beinsensitive to the defocus, and the spatial resolution may not be limited bythe spherical and the chromatic aberrations of objective lens. Therefore, theimaging of small molecules, such as, the drug structure will bestraightforward. By taking multiple projection images at the different zoneaxes from many micro-crystals, or from surrounding thin edges of a largecrystal, we may reconstruct 3D structure of the larger protein complex inatomic resolution.

Proposal of Bragg Diffraction Imaging on Protein Crystals with Precession-Electron Annular-Bright-Field Microscopy