Diffracted Atoms: The Economy of X-Ray Crystallography

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You cannot see a virus with a microscope. You must freeze it into a crystal, blast it with X-rays, and use a supercomputer to translate the scattered radiation into a 3D map of its atoms.
You cannot put a virus or a complex protein under a standard microscope and look at it. The wavelength of visible light is simply too large to resolve individual atoms. To see the physical shape of the biological molecules that cause disease, the global pharmaceutical industry relies on the extreme, high-energy physics of X-Ray Crystallography. This technical reference details the brutal physics required to image the invisible. Biochemists must first force organic, squishy proteins to form perfect, solid geometric crystals—an agonizing process that can take years. Once crystallized, scientists blast the sample with intense X-ray beams. As the X-rays hit the densely packed atoms, they diffract, scattering onto a detector plate in a complex, seemingly chaotic pattern of dots. We analyze the staggering supercomputing power and Fourier transform mathematics required to read these scattered dot patterns and reverse-engineer them into a flawless, 3D atomic map. This is the exact technology used to discover the structure of DNA and design targeted modern cancer drugs. See the invisible architecture of disease. Learn how physicists turn biological tissue into glass and shoot it with radiation to map the precise coordinates of every single atom.

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Michael Chavez
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x-ray crystallography physics protein structure atomic mapping pharmaceutical biochemistry molecular structure algorithms dna double helix discovery biomedical research crystal diffraction

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