Mariyuki



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Fastest X-ray images of tiny biological crystals
"An international research team headed by DESY scientists from the Center  for Free-Electron Laser Science (CFEL) in Hamburg, Germany, has  recorded the shortest X-ray exposure of a protein crystal ever achieved.  The incredible brief exposure time of 0.000 000 000 000 03 seconds (30  femtoseconds) opens up new possibilities for imaging molecular processes  with X-rays.
The molecular structure of proteins is inferred by X-ray diffraction  from crystals composed of building blocks of identical protein  molecules.  This image shows the amount of atomic disordering that  occurs in such a protein crystal when illuminated by an ultra-intense  pulse from an X-ray free-electron laser. The disordering increases with  time (depicted by colour changing from blue to red). The crystal becomes  an amorphous soup of atoms by the end of the pulse, which no longer  gives strong diffraction peaks. The diffraction peaks at high resolution  turn off early in the pulse, whereas low-resolution diffraction lasts  longer. Even if pulses are much longer than the explosion timescale, the  measurement corresponds to the undamaged molecule.
Credit: Carl Caleman  and Anton Barty, CFEL/DESY”

via desy

I´d love to try this with my proteins!
:-O

Fastest X-ray images of tiny biological crystals

"An international research team headed by DESY scientists from the Center for Free-Electron Laser Science (CFEL) in Hamburg, Germany, has recorded the shortest X-ray exposure of a protein crystal ever achieved. The incredible brief exposure time of 0.000 000 000 000 03 seconds (30 femtoseconds) opens up new possibilities for imaging molecular processes with X-rays.

The molecular structure of proteins is inferred by X-ray diffraction from crystals composed of building blocks of identical protein molecules. This image shows the amount of atomic disordering that occurs in such a protein crystal when illuminated by an ultra-intense pulse from an X-ray free-electron laser. The disordering increases with time (depicted by colour changing from blue to red). The crystal becomes an amorphous soup of atoms by the end of the pulse, which no longer gives strong diffraction peaks. The diffraction peaks at high resolution turn off early in the pulse, whereas low-resolution diffraction lasts longer. Even if pulses are much longer than the explosion timescale, the measurement corresponds to the undamaged molecule.

Credit: Carl Caleman and Anton Barty, CFEL/DESY”

via desy

I´d love to try this with my proteins!

:-O

01:29 pm, by mariyuki23 notes Comments