PubMed | Lawrence Livermore National Laboratory, 1 Max Planck Institute For Medizinische Forschung, University of Chicago, Max Planck Institute for Nuclear Physics and 7 more.
Type: Journal Article | Journal: Nature methods | Year: 2014
We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a protein quake: the hypothesis that proteins rapidly dissipate energy through quake-like structural motions.
PubMed | Lawrence Livermore National Laboratory, 1 Max Planck Institute For Medizinische Forschung, University of Hamburg, Uppsala University and 5 more.
Type: | Journal: Nature communications | Year: 2013
Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 resolution and determine its serial femtosecond crystallography structure to 3.5 resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.