Final answer:
X-rays are preferred for diffraction patterns of protein crystals because their wavelength matches the size of atoms, making them suitable for X-ray diffraction to detect crystal structure and atomic arrangement, crucial in scientific breakthroughs like the discovery of DNA's structure.
Step-by-step explanation:
X-rays are the preferred type of electromagnetic radiation used to produce diffraction patterns of protein crystals primarily because the wavelength of a typical X-ray corresponds to the length of a covalent bond, which is on the order of the size of atoms and small molecules. This makes X-rays ideally suited for studying the structure of crystals, including protein crystals, through a process known as X-ray diffraction. By measuring the angles and intensities of the diffracted X-ray beams, researchers can create a detailed map of the electron density within the crystal and infer the arrangement of atoms in a protein, often leading to a precise atomic model.
X-ray diffraction patterns have played a crucial role in molecular biology, most famously in the determination of the double-helix structure of DNA by Crick, Watson, and Wilkins, who were later awarded the Nobel Prize in Physiology or Medicine for their discovery. This scientific achievement was heavily reliant on the X-ray diffraction data supplied by Rosalind Franklin. In the field of Physics and Materials Science, the technique continues to be invaluable in the study of atomic arrangements in complex materials, such as high-temperature superconductors, which has important applications in the development of new materials.