Crystallography[edit | edit source]
Crystallography is the experimental science of determining the arrangement of atoms in solids. In older usage, it is the scientific study of crystals.
Before the development of X-ray diffraction crystallography (see below), the study of crystals was based on the geometry of the crystals. This involves measuring the angles of crystal faces relative to theoretical reference axes (crystallographic axes), and establishing the symmetry of the crystal in question. The former is carried out using a goniometer. The position in 3D space of each crystal face is plotted on a stereographic net, e.g. Wolff net or Lambert net. In fact, the pole to each face is plotted on the net. Each point is labelled with its Miller index. The final plot allows the symmetry of the crystal to be established.
Crystallographic methods now depend on the analysis of the diffraction patterns that emerge from a sample that is targeted by a beam of some type. The beam is not always electromagnetic radiation, even though X-rays are the most common choice. For some purposes electrons or neutrons are used, which is possible due to the wave properties of the particles. Crystallographers often explicitly state the type of illumination used when referring to a method, as with the terms X-ray diffraction, neutron diffraction and electron diffraction.
These three types of radiation interact with the specimen in different ways. X-rays interact with the spatial distribution of the valence electrons, while electrons are charged particles and therefore feel the total charge distribution of both the atomic nuclei and the surrounding electrons. Neutrons are scattered by the atomic nuclei through the strong nuclear forces, but in addition, the magnetic moment of neutrons is non-zero. They are therefore also scattered by magnetic fields. Because of these different forms of interaction, the three types of radiation are suitable for different crystallographic studies.
In several cases, an image of a microscopic object is generated by focusing the rays of the visible spectrum using a lens as in light microscopy. However, because the wavelength of visible light is long compared to atomic bond lengths and atoms themselves, it is necessary to use radiation with shorter wavelengths, such as X-rays. Employing shorter wavelengths implies abandoning microscopy and true imaging, however, because there exists no material from which a lens capable of focusing this type of radiation can be created. (That said, scientists have had some success focusing X-rays with microscopic Fresnel zone plates made from gold). Generally, in diffraction-based imaging, the only wavelengths used are those that are too short to be focused. This difficulty is the reason that crystals must be used.
Because of their highly ordered and repetitive structure, crystals are an ideal material for analyzing the structure of solids. To use X-ray diffraction as an example, a single X-ray photon diffracting off of one electron cloud will not generate a strong enough signal for the equipment to detect. However, many X-rays diffracting off many electron clouds in approximately the same relative position and orientation throughout the crystal will result in constructive interference and hence a detectable signal.
Crystallography is a tool that is often employed by materials scientists. In single crystals, the effects of the crystalline arrangement of atoms is often easy to see macroscopically, because the natural shapes of crystals reflect the atomic structure. In addition, physical properties are often controlled by crystalline defects. The understanding of crystal structures is an important prerequisite for understanding crystallographic defects. Mostly, materials do not occur in a syngle crystalline, but poly-crystalline form, such that the powder diffraction method plays a most important role in structural determination.
A number of other physical properties are linked to crystallography. For example, the minerals in clay form small, flat, platelike structures. Clay can be easily deformed because the platelike particles can slip along each other in the plane of the plates, yet remain strongly connected in the direction perpendicular to the plates. Such mechanisms can be studied by crystallographic texture measurements.
In another example, iron transforms from a body-centered cubic (bcc) structure to a face-centered cubic (fcc) structure called austenite when it is heated. The fcc structure is a close-packed structure, and the bcc structure is not, which explains why the volume of the iron decreases when this transformation occurs.
Crystallography is useful in phase identification: That is, when performing some kind of processing on a material, it is often desired to find out what compounds and what phases are present in the material. Each phase has a characteristic arrangement of atoms. Techniques like X-ray diffraction can be used to identify which patterns are present in the material, and thus which compounds are present (note: the determination of the "phases" within a material should not be confused with the more general problem of "phase determination," which refers to the phase of waves as they diffract from planes within a crystal, and which is a necessary step in the interpretation of complicated diffraction patterns).
Crystallography covers the enumeration of the symmetry patterns which can be formed by atoms in a crystal and for this reason has a relation to group theory and geometry. See symmetry group.
X-ray crystallography is the primary method for determining the molecular conformations of biological macromolecules, particularly protein and nucleic acids such as DNA and RNA. In fact, the double-helical structure of DNA was deduced from crystallographic data. The first crystal structure of a macromolecule was solved in 1958 (Kendrew, J.C. et al. (1958) A three-dimensional model of the myoglobin molecule obtained by X-ray analysis (Nature 181, 662–666). The Protein Data Bank (PDB) is a freely accessible repository for the structures of proteins and other biological macromolecules. RasMol can be used to visualize biological molecular structures.
Electron crystallography has been used to determine some protein structures, most notably membrane proteins and viral capsids.