Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and its 146 kDa Complex With HPr Using Residual Dipolar Couplings and Small and Wide Angle X-Ray Scattering

Lignende værker

• Combined Use of Residual Dipolar Couplings and Solution X-ray Scattering to Rapidly Probe Rigid Body Conformational Transitions in a Non-Phosphorylatable Active Site Mutant of the 128 kDa Enzyme I Dimer
  af: Takayama, Yuki, et al.
  Udgivet: (2010)
• Solution NMR Structure of the 48-kDa IIA(Mannose)-HPr Complex of the Escherichia coli Mannose Phosphotransferase System
  af: Williams, David C., et al.
  Udgivet: (2005)
• Dynamic equilibrium between closed and partially closed states of the bacterial Enzyme I unveiled by solution NMR and X-ray scattering
  af: Venditti, Vincenzo, et al.
  Udgivet: (2015)
• Quantitative Characterization of Configurational Space Sampled by HIV-1 Nucleocapsid Using Solution NMR, X-ray Scattering and Protein Engineering
  af: Deshmukh, Lalit, et al.
  Udgivet: (2016)
• Using Small Angle Solution Scattering Data in Xplor-NIH Structure Calculations
  af: Schwieters, Charles D., et al.
  Udgivet: (2014)