HAMBURG, Germany, Nov. 14, 2006 -- Using a single, extremely short and intense x-ray laser pulse, an international team of scientists have, for the first time, taken a high-resolution diffraction image of an object such as a protein before the intensity of the radiation destroyed the sample. The experiment was the first successful application of "flash diffractive imaging" and begins a new era in structural research.
The new method will be applicable to atomic-resolution imaging of complex biomolecules when even more powerful x-ray lasers, currently under construction, are available. The technique will allow scientists to gain insight into the fields of materials science, plasma physics, biology and medicine.
The scientists, part of an international collaboration led by Lawrence Livermore National Laboratory's (LLNL) Henry Chapman and Janos Hajdu of Uppsala University in Sweden, achieved the feat using the world's first soft x-ray free-electron laser, located at the FLASH facility at Deutsches Elektronen-Synchrotron (DESY) in Hamburg. Their work will appear on the cover of the December issue of the journal Nature Physics (12 November 2006 | doi:10.1038/nphys461).
The experiment suggests that in the near future, images from nanoparticles and even large individual macromolecules -- viruses or cells -- may be obtained using a single, ultrashort high-intensity laser pulse before the sample explodes and turns into a plasma. This means that scientists could better understand the structure of macromolecular proteins without crystallizing them, which is required in conventional x-ray structure analysis, and have the ability to rapidly study all classes of proteins.