Paramagnetic Ions Provide Structural Restraints in Solid-State NMR of Proteins

2007 ◽  
Vol 129 (8) ◽  
pp. 2218-2219 ◽  
Author(s):  
Stéphane Balayssac ◽  
Ivano Bertini ◽  
Moreno Lelli ◽  
Claudio Luchinat ◽  
Massimiliano Maletta
2016 ◽  
Vol 18 (14) ◽  
pp. 9752-9757 ◽  
Author(s):  
Wenyu Li ◽  
Vinicius R. Celinski ◽  
Johannes Weber ◽  
Nathalie Kunkel ◽  
Holger Kohlmann ◽  
...  

Paramagnetic doping homogeneity can be elucidated by quantitative solid-state NMR experiments.


2020 ◽  
Author(s):  
Maximilian Zinke ◽  
Katrin A. A. Sachowsky ◽  
Carl Öster ◽  
Sophie Zinn-Justin ◽  
Raimond B.G. Ravelli ◽  
...  

AbstractPhage therapy has recently regained attention at combating multidrug-resistant bacteria. In 2019, tailed bacteriophages of the Siphoviridae family were engineered to successfully treat a disseminated bacterial infection after all other drugs had failed.(1) This family of phages features a long, flexible, non-contractile tail that has been difficult to characterize structurally. Here, we present the atomic structure of the tail-tube of the bacteriophage SPP1 – a member of this family. Our hybrid structure is based on the integration of structural restraints from solid-state NMR and a density map from cryo-EM. We show that the tail tube protein (TTP) gp17.1 organizes into hexameric rings that are stacked by flexible linker domains and, thus, form a hollow flexible tube with a negatively charged lumen suitable for the transport of DNA.One sentence summaryIntegrative structural biology by solid-state NMR and cryo-EM enables structure determination of the flexible tail of the bacteriophage SPP1.


2012 ◽  
Vol 134 (22) ◽  
pp. 9022-9025 ◽  
Author(s):  
Thach V. Can ◽  
Mukesh Sharma ◽  
Ivan Hung ◽  
Peter L. Gor’kov ◽  
William W. Brey ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document