NMR Ensembles of Models: Difference between revisions
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==Reliability of NMR Models== | ==Reliability of NMR Models== | ||
NMR models are more likely to contain major errors <ref>Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. Sander B. Nabuurs, Chris. A. E. M. Spronk, Geerten W. Vuister, and Gert Vriend. (2006). PLoS Computational Biology 2: [http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0020009 Open Access Full Text] [http://proteinexplorer.org/favlit/nmr.htm Precis]. DOI: 10.1371/journal.pcbi.0020009</ref> than are crystallographic models that have good [[Resolution]] and [[Free R]] values. See also [[Quality assessment for molecular models]]. | NMR models are more likely to contain major errors <ref>Traditional biomolecular structure determination by NMR spectroscopy allows for major errors. Sander B. Nabuurs, Chris. A. E. M. Spronk, Geerten W. Vuister, and Gert Vriend. (2006). PLoS Computational Biology 2: [http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.0020009 Open Access Full Text] [http://proteinexplorer.org/favlit/nmr.htm Precis]. DOI: 10.1371/journal.pcbi.0020009</ref> than are crystallographic models that have good [[Resolution]] and [[Free R]] values. See also [[Quality assessment for molecular models]]. In 2012, an X-ray crystallographic structure of integral membrane diacylglycerol kinase, [[3ze4]], revealed functionally important domain swapping that was not present in an earlier NMR structure [[2kdc]]<ref>PMID: 19556511</ref>. | ||
==Median Size of Published NMR Structures== | ==Median Size of Published NMR Structures== | ||
