Current Option of Structural Biology: What Can X-ray Diffraction Do?

 

Chun-Jung Chen

X-ray Structural Biology Research Division, Synchrotron Radiation Research Center, Hsinchu 300, Taiwan.

 

X-rays constitute the region of the electromagnetic spectrum that lies between the ultraviolet and gamma ray, which makes it especially useful in imaging a molecule or material because their wavelengths, ranging from 0.01 to 100Å, are comparable to or smaller than the atoms making up the molecule.  Since 1991, the increase use of synchrotron radiation facilities, which offer X-ray beams that are tunable and many times more brilliant than those from laboratory sources, has been playing a key role on structural biology research, such as X-ray crystallography, non-crystalline diffraction, absorption spectroscopy and microscopy imaging.  The function of a gene product is tightly coupled to its three-dimensional structure, thus determining the structure, or its folding pattern, may provide important insight into its biochemical function, which is especially important for “structural genomics” where an industrialization of the crystallographic process could lead to the production of a massive number of structures.  In this talk, X-ray protein crystallography using the power of traditional X-ray source and synchrotron radiation to facilitate structure determinations in structural biology will be mainly described.

 

 

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