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The role of flexibility and molecular shape in the crystallization of proteins by surface mutagenesis
Proteins are dynamic systems and interact with their environment. The analysis of crystal contacts in the most accurately determined protein structures (d < 1.5 Å) reveals that in contrast to current views, static disorder and high side-chain entropy are common in the crystal contact area. These...
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| Pubblicato in: | Acta Crystallogr F Struct Biol Commun |
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| Autore principale: | |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
International Union of Crystallography
2015
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4321469/ https://ncbi.nlm.nih.gov/pubmed/25664789 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2053230X14027861 |
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