Final answer:
X-ray crystallography is a technique used to determine the structure of crystals, including proteins like hen egg lysozyme, by analyzing the diffraction patterns of X-rays scattered through them. This method provides detailed information on the atomic and molecular arrangement within the crystal.
Step-by-step explanation:
The process depicted in the figures is known as X-ray crystallography. It is a method used to determine the atomic and molecular structure of a crystal, in which the crystalline atoms cause a beam of incident X-rays to diffract into many specific directions.
By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their disorder, and various other information.
Historically, X-ray crystallography has been fundamental in the development of many scientific fields. For example, it was instrumental in discerning the double helix structure of DNA, based on the X-ray diffraction data provided by Rosalind Franklin to Watson and Crick.
Currently, this technique is also critical in researching materials such as high-temperature superconductors. The diffraction pattern from hen egg lysozyme, as shown in the figures, illustrates the interference pattern obtained during X-ray crystallography, analysis of which yields information about the protein's structure.