We have not synchrotron center in our region, so it is important for us to obtain certainty about the protein crystals quality before x-ray diffraction.
You could check if the crystal is salt or protein using dye methods or running on sds-page. If it is protein, you could check if it is diffracting to a good resolution, u just need a in-house X-ray source nearby. It takes only a few minutes to know if your crystal is diffracting well, then you could send it to a synchotron for data collection..
If your believe the protein might be proteolytically cleaved while in the crystallization drop, you can take a crystal (from a well with more than one), dissolve it in some buffer, and acquire a mass spectrum for the dissolved crystal. If you see peaks at molecular weights other than the weights of the macromolecules in your drop, then you know something has happened to the protein during crystallization. You can also use dissolved crystals for SDS-PAGE or native PAGE if those types of analysis would be beneficial for you. There's no way to determine how well the crystal will diffract without mounting it on some kind of x-ray source, however. If you have a rotating anode diffraction system at your university, then acquire a few images. If they look good, unmount the crystal (while keeping it frozen at all times!) and send it to a synchrotron to collect a full set of data.
We have XRD and XRF system in our university but as I know those are not proper for soft material like protein because the sample preparation problems. would you please introduce me a reference about rotating anode diffraction ( in-house X-ray source) application in this case?
Is microscopy technique useable for this propose?
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