Вставка
- Опубліковано 29 січ 2020
- Proteins are really tiny, and therefore too small for light microscopy. Thus we need other methods for looking at them: X-ray crystallography.🔍
To do so, crystals of the protein of interest are grown by screening large amounts of growth conditions in 96-well screening plates. Protein crystal are formed by regular and symmetric arrangement of a protein. At a particle accelerator (synchroton light source), we measure cryo-cooled crystals to see the interactions of X-rays with the crystalline material. The nearest synchroton is in Villigen.
To carry the crystals there safely, we fish them with tiny nylon loops and flash freeze❄ them in liquid nitrogen. You probably wonder how?
The 96-well screens containing the crystals are stored in an automatic, temperature controlled incubator. We retrieve the screens and search for crystals under a microscope. Well, once we find crystals (lucky us 😜), we cut open the cover of the screening plate, (gu)estimate the size of the crystal, pick a suitable loop and fish the crystals with the loop. Cryoprotectants help keeping the crystals intact before we flash freeze them in liquid nitrogen. But beware: Ice crystals❄ disturb the measurement! Thus, the containers for storing and transporting them need to be cooled with liquid nitrogen beforehand and kept closed to avoid ice crystal formation. After fishing up to 16 crystals into one container, we close it, put it back into a liquid nitrogen tank, return the screens and then… off we go to Villigen!
Have a nice Thursday
#NCCR #NCCRmse #crystal #structuralbiology #fishing #Xray - Наука та технологія
