X-ray crystallography
hideX-ray crystallography is a method of determining the arrangement of atoms within a crystal, in which a beam of X-rays strikes a crystal and diffracts into many specific directions. From 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.
Since many materials can form crystals — such as salts, metals, minerals, semiconductors, as well as various inorganic, organic and biological molecules — X-ray crystallography has been fundamental in the development of many scientific fields. In its first decades of use, this method determined the size of atoms, the lengths and types of chemical bonds, and the atomic-scale differences among various materials, especially minerals and alloys. The method also revealed the structure and functioning of many biological molecules, including vitamins, drugs, proteins and nucleic acids such as DNA. X-ray crystallography is still the chief method for characterizing the atomic structure of new materials and in discerning materials that appear similar by other experiments. X-ray crystal structures can also account for unusual electronic or elastic properties of a material, shed light on chemical interactions and processes, or serve as the basis for designing pharmaceuticals against diseases.
In an X-ray diffraction measurement, a crystal is mounted on a goniometer and gradually rotated while being bombarded with X-rays, producing a diffraction pattern of regularly spaced spots known as reflections. The two-dimensional images taken at different rotations 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.
X-ray crystallography is related to several other methods for determining atomic structures. Similar diffraction patterns can be produced by scattering electrons or neutrons, which are likewise interpreted as a Fourier transform. If single crystals of sufficient size cannot be obtained, various other X-ray methods can be applied to obtain less detailed information; such methods include fiber diffraction, powder diffraction and small-angle X-ray scattering (SAXS). In all these methods, the scattering is elastic; the scattered X-rays have the same wavelength as the incoming X-ray. By contrast, inelastic X-ray scattering methods are useful in studying excitations of the sample, rather than the distribution of its atoms.
For more information about X-ray crystallography, read the full article at
Wikipedia.
This text uses material from Wikipedia and is available under the GNU Free Documentation License.
News tagged with x ray crystallography
Computational microscope peers into the working ribosome (w/ Video)
Nov 23, 2009 |
4.9 / 5 (9) |
2
Two new studies reveal in unprecedented detail how the ribosome interacts with other molecules to assemble new proteins and guide them toward their destination in biological cells. The studies used molecular ...
Biologists reveal structure of cell nucleus 'gatekeeper'
Oct 27, 2009 |
4 / 5 (5) |
6
(PhysOrg.com) -- Biologists led by associate professor Thomas Schwartz (MIT) have worked out a rudimentary architectural plan for the nuclear pore complex (NPC), the gatekeeper of the cell's nucleus.
2 Americans, 1 Israeli win Nobel chemistry prize
Oct 07, 2009 |
5 / 5 (3) |
1
(AP) -- Two Americans and an Israeli scientist won the 2009 Nobel Prize in chemistry on Wednesday for atom-by-atom mapping of the protein-making factories within cells - a feat that has spurred the development ...
Disordered proteins sensitive to environment, sequence changes
Sep 14, 2009 |
not rated yet |
0
(PhysOrg.com) -- Research published by a team of Indiana University bioinformaticists has shown quantitatively the influence of small sequence changes and environmental conditions on the disordered regions ...
Boron-based compounds trick a biomedical protein
Sep 07, 2009 |
not rated yet |
0
(PhysOrg.com) -- Chemists and biologists have successfully demonstrated that specially synthesized boron compounds are readily accepted in biologically active enzymes, a move that, they say, is a proof of concept that could ...
Boron-based compounds trick a biomedical protein
Sep 02, 2009 |
5 / 5 (1) |
0
Chemists and biologists have successfully demonstrated that specially synthesized boron compounds are readily accepted in biologically active enzymes, a move that, they say, is a proof of concept that could ...
Fighting disease atom by atom: Atomic map of hepatitis E may reveal strategies to fight it
Jul 21, 2009 |
5 / 5 (2) |
0
Researchers at Rice University and their international colleagues have for the first time described the atomic structure of the protein shell that carries the genetic code of hepatitis E (HEV). Their findings, ...
Antibody key to treating variant CJD, scientists find
Mar 04, 2009 |
5 / 5 (3) |
0
Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.
Forgotten and lost - when proteins 'shut down' our brain
Biology /
Feb 17, 2009 |
3.5 / 5 (4) |
0
(PhysOrg.com) -- Which modules of the tau protein, in neurons of Alzheimer disease patients, may act in a destructive manner were investigated by researchers from the Max Planck Institute for Biophysical Chemistry ...
Sticky antibodies block prion disease
Biology /
Feb 12, 2009 |
5 / 5 (1) |
0
(PhysOrg.com) -- Antibodies that stick to a brain prion protein called PrP could be the key to treating prion diseases like variant CJD and preventing people accidentally exposed to prions from going on to ...
Groundbreaking study on complex movements of enzymes
Biology /
Feb 11, 2009 |
4 / 5 (1) |
0
A groundbreaking study has revealed in great detail how enzymes in the cell cooperate to make fat. These enzymes are integrated into a single molecular complex known as fatty acid synthase. This complex is regarded as a potential ...
Dartmouth researchers find new protein function
Biology /
Jan 09, 2009 |
4 / 5 (1) |
0
A group of Dartmouth researchers has found a new function for one of the proteins involved with chromosome segregation during cell division. Their finding adds to the growing knowledge about the fundamental ...


