Difference between revisions of "Macromolecular Crystallography"
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Revision as of 10:36, 4 February 2015
Macromolecular Crystallography (sometimes abbreviated as MX) is the measurement of single-crystal diffraction patterns, in order to solve for the three-dimensional structure of macromolecules. The sample-of-interest is almost always a protein. Macromolecular crystallography is thus a powerful tool for resolving the three-dimensional structure of proteins, including studying their conformational changes when binding small molecules, or associating with other proteins.
Literature
- Chayen NE, Boggon TJ, Cassetta A, Deacon A, Gleichmann T, Habash J, Harrop SJ, Helliwell JR, Nieh YP, Peterson MR, Raftery J, Snell EH, Hädener A, Niemann AC, Siddons DP, Stojanoff V, Thompson AW, Ursby T, Wulff M Trends and Challenges in Experimental Macromolecular Crystallography Quarterly Reviews of Biophysics 1996, 29 (03), 227-278. doi: 10.1017/S0033583500005837
- John R. Helliwell and Edward P. Mitchell Synchrotron radiation macromolecular crystallography: science and spin-offs IUCrJ 2015, 2 (2). doi: 10.1107/S205225251402795X
Serial Crystallography using Free-Electron Lasers (FELs)
- Ilme Schlichting Serial femtosecond crystallography: the first five years IUCrJ 2015, 2 (2). doi: 10.1107/S205225251402702X
