Difference between revisions of "Macromolecular Crystallography"

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'''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.
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'''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 ('''protein crystallography''', '''PX'''). 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==
 
==Literature==

Latest revision as of 10:44, 10 March 2017

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 (protein crystallography, PX). 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

See Also

See Also