Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites

The JCSG has recently developed a protocol for systematic comparisons of high-quality crystal and NMR structures of proteins. In this paper, the extent to which this approach can provide function-related information on the two functionally annotated proteins TM1081, a Thermotoga maritima anti-σ fact...

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Detalles Bibliográficos
Autores principales: Serrano, Pedro, Pedrini, Bill, Geralt, Michael, Jaudzems, Kristaps, Mohanty, Biswaranjan, Horst, Reto, Herrmann, Torsten, Elsliger, Marc-André, Wilson, Ian A., Wüthrich, Kurt
Formato: Texto
Lenguaje:English
Publicado: International Union of Crystallography 2010
Materias:
NMR in a high-throughput environment
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954230/
https://www.ncbi.nlm.nih.gov/pubmed/20944236
http://dx.doi.org/10.1107/S1744309110033658

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954230/
https://www.ncbi.nlm.nih.gov/pubmed/20944236
http://dx.doi.org/10.1107/S1744309110033658

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