25 Facts About X-ray diffraction

Since many materials can form crystals—such as salts, metals, minerals, semiconductors, as well as various inorganic, organic, and biological molecules—X-ray diffraction crystallography has been fundamental in the development of many scientific fields.

X-ray diffraction crystallography is still the primary method for characterizing the atomic structure of new materials and in discerning materials that appear similar by other experiments.

X-ray diffraction crystallography is related to several other methods for determining atomic structures.

Just as an ocean wave striking a lighthouse produces secondary circular waves emanating from the lighthouse, so an X-ray diffraction striking an electron produces secondary spherical waves emanating from the electron.

In principle, any wave impinging on a regular array of scatterers produces X-ray diffraction, as predicted first by Francesco Maria Grimaldi in 1665.

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Structure of graphite was solved in 1916 by the related method of powder X-ray diffraction, which was developed by Peter Debye and Paul Scherrer and, independently, by Albert Hull in 1917.

X-ray diffraction crystallography has led to a better understanding of chemical bonds and non-covalent interactions.

Finally, X-ray diffraction crystallography had a pioneering role in the development of supramolecular chemistry, particularly in clarifying the structures of the crown ethers and the principles of host–guest chemistry.

X-ray diffraction is a very powerful tool in catalyst development.

Single-crystal X-ray diffraction is used in the pharmaceutical industry, due to recent problems with polymorphs.

Since the 1920s, X-ray diffraction has been the principal method for determining the arrangement of atoms in minerals and metals.

X-ray diffraction crystallography is used routinely to determine how a pharmaceutical drug interacts with its protein target and what changes might improve it.

In general, single-crystal X-ray diffraction offers more structural information than these other techniques; however, it requires a sufficiently large and regular crystal, which is not always available.

Neutron X-ray diffraction is an excellent method for structure determination, although it has been difficult to obtain intense, monochromatic beams of neutrons in sufficient quantities.

In general, small molecules are easier to crystallize than macromolecules; however, X-ray diffraction crystallography has proven possible even for viruses and proteins with hundreds of thousands of atoms, through improved crystallographic imaging and technology.

X-ray diffraction beams generated in large machines called synchrotrons which accelerate electrically charged particles, often electrons, to nearly the speed of light and confine them in a circular loop using magnetic fields.

Data collected from a X-ray diffraction experiment is a reciprocal space representation of the crystal lattice.

The intensity of each X-ray diffraction 'spot' is recorded, and this intensity is proportional to the square of the structure factor amplitude.

Main goal of X-ray diffraction crystallography is to determine the density of electrons f throughout the crystal, where r represents the three-dimensional position vector within the crystal.

An intuitive understanding of X-ray diffraction can be obtained from the Bragg model of diffraction.

The orientation of a particular set of sheets is identified by its three Miller indices, and let their spacing be noted by d William Lawrence Bragg proposed a model in which the incoming X-rays are scattered specularly from each plane; from that assumption, X-rays scattered from adjacent planes will combine constructively when the angle ? between the plane and the X-ray results in a path-length difference that is an integer multiple n of the X-ray wavelength ?.

X-ray diffraction has wide and various applications in the chemical, biochemical, physical, material and mineralogical sciences.

X-ray diffraction is analogous to a microscope with atomic-level resolution which shows the atoms and their electron distribution.

X-ray diffraction has been used for the identification of antibiotic drugs such as: eight ß-lactam, three tetracycline and two macrolide antibiotic drugs.

X-ray diffraction has been demonstrated as a method for investigating the complex structure of integrated circuits.

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