Building on previous work (Uervirojnangkoorn et al., 2015), we demonstrate how improved methods for processing XFEL diffraction data enable the determination of structures from poorly diffracting crystals.
The conformations of the enzyme cyclophilin A that are essential for its catalytic activity are temperature dependent and exhibit diverse responses, which is consistent with a complex energy landscape.
A combination of molecular dynamics simulations and X-ray diffraction data has been used to construct more realistic models of proteins and to provide new insights into their interactions with other proteins and biomolecules.
A comprehensive structural analysis of inhibitory murine antibody 3D11 binding to Plasmodium berghei circumsporozoite protein reveals common mechanisms of antibody evolution in mammals against Plasmodium parasites.
Molecular simulations, small-angle X-ray and neutron scattering experiments and previously measured NMR experiments were combined to study the structure and dynamics of the proteins and lipids in a nanodisc.