Pharmaceutical X-Ray Diffraction (XRD)

X-ray crystallography, also known as X-ray Diffraction (XRD), is the science of determining the atomic and molecular structure of a crystal using a beam of X-rays. While often used on synthetic compounds, XRD can also be used to determine the crystal structures of proteins, nucleic acids and other biological molecules for biologics manufacturers.

How to XRDs Work?

X-Ray Diffractometers measure the angels and amplitudes of x-rays diffracted by molecular bonds within crystalline solids, in the pharmaceutical industry their main purpose being the characterization of the properties of solid drug compounds. In a single-crystal X-ray diffraction measurement, a crystal is mounted on a goniometer. The goniometer is used to position the crystal at selected orientations. The crystal is illuminated with a finely focused monochromatic beam of X-rays, producing a diffraction pattern of regularly spaced spots known as reflections. The two-dimensional images taken at different orientations are converted into a three-dimensional model of the density of electrons within the crystal using the mathematical method of Fourier transforms, combined with chemical data known for the sample. Poor resolution (fuzziness) or even errors may result if the crystals are too small, or not uniform enough in their internal makeup.