Science Impact

Outrunning X-ray radiation damage with the use of X-ray FELs, like LCLS, enables the determination of room temperature metalloprotein structures.

An optical laser (green) exciting the iron-containing active site of the protein cytochrome c, and then an X-ray laser (white) probing the iron a few femtoseconds to picoseconds later

Measuring X-ray diffraction from nanocrystals using X-ray FELs like LCLS allows structures of difficult-to-crystallize proteins to be determined.

Arrestin (yellow), an important type of signaling protein, while docked with rhodopsin (orange), a G protein-coupled receptor.

LCLS has allowed studying the active state structure of photosensitive proteins from femto- to milliseconds after photoactivation.

A protein from photosynthetic bacteria changing shape in response to light

X-ray free electron lasers likeĀ  LCLS have become vital for studying the structural rearrangements in enzymes during biological reactions.

X-rays passing through a crystal to form an intensity pattern on a detector behind the crystal that is dominated by bright spots

Solving structures at ambient temperature with minimal radiation damage through LCLS provides more accurate information on binding pockets.

Crystallized ribosomes traveling through a capillary into the interaction region, where they are zapped with a beam of X-rays