X-ray crystallography
From Proteopedia
(Difference between revisions)
												
			
			|  (→See Also - adding content) |  (→See Also - polishing) | ||
| Line 14: | Line 14: | ||
| *[http://en.wikipedia.org/wiki/X-ray_crystallography X-ray Crystallography at Wikipedia] | *[http://en.wikipedia.org/wiki/X-ray_crystallography X-ray Crystallography at Wikipedia] | ||
| *[http://hamptonresearch.com/gallery.aspx Protein Crystal Gallery] | *[http://hamptonresearch.com/gallery.aspx Protein Crystal Gallery] | ||
| + | |||
| *[[Quality assessment for molecular models]] | *[[Quality assessment for molecular models]] | ||
Revision as of 00:24, 19 May 2009
|   | 
| Flow chart showing the major steps in X-ray protein crystallography. (Image from Wikimedia courtesy Thomas Splettstoesser. | 
About 85% of the models (entries) in the World Wide Protein Data Bank were determined by X-ray crystallography. (Most of the remaining 15% were determined by solution nuclear magnetic resonance.) Protein crystallography remains very difficult, despite many recent advances. For every new protein sequence targeted for X-ray crystallography, about one in twenty is solved[1][2]. Publication of solved structures involves depositing an atomic coordinate file (PDB file) in the World Wide Protein Data Bank.
See Also
Further Reading
- Crystallography Made Crystal Clear: a guide for users of macromolecular models, a book by Gale Rhodes.
