X-ray crystallography
From Proteopedia
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*[[Highest impact structures]] of all time. | *[[Highest impact structures]] of all time. | ||
*[[Nobel Prizes for 3D Molecular Structure]] | *[[Nobel Prizes for 3D Molecular Structure]] | ||
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| + | ==Further Reading== | ||
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| + | *[http://www.pdb.org/pdb/static.do?p=general_information\about_pdb\nature_of_3d_structural_data.html Crystallography Made Crystal Clear: a guide for users of macromolecular models], a book by Gale Rhodes. | ||
==Notes & References== | ==Notes & References== | ||
<references /> | <references /> | ||
Revision as of 21:11, 18 May 2009
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| 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.
