| Literature DB >> 25984698 |
Mohammed Kaplan1, Abhishek Cukkemane1, Gydo C P van Zundert1, Siddarth Narasimhan1, Mark Daniëls1, Deni Mance1, Gabriel Waksman2, Alexandre M J J Bonvin1, Rémi Fronzes3, Gert E Folkers1, Marc Baldus1.
Abstract
Studying biomolecules at atomic resolution in their native environment is the ultimate aim of structural biology. We investigated the bacterial type IV secretion system core complex (T4SScc) by cellular dynamic nuclear polarization-based solid-state nuclear magnetic resonance spectroscopy to validate a structural model previously generated by combining in vitro and in silico data. Our results indicate that T4SScc is well folded in the cellular setting, revealing protein regions that had been elusive when studied in vitro.Mesh：
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Year: 2015 PMID： 25984698 DOI： 10.1038/nmeth.3406
Source DB: PubMed Journal: Nat Methods ISSN： 1548-7091 Impact factor: 28.547