 |
 |
So, if you are bored and have nothing else to do (which is how we all are at times; kidding), can you set up a control experiment with everything in the crystal dip except protein (so buffer and whatever)? I know protein plays a role in the process, but I have done this before when I had suspect conditions, and it did show that my buffer formed crystals in that situation. Sometimes it helps. But I am one that never throws a crystal away, and always just puts it in a beam before saying it's salt. Protein crystals are too precious to rule out by over thinking. Good luck Dave On 2/8/2013 9:13 AM, Edward A. Berry wrote: > Raji Edayathumangalam wrote: >> (3) Inconclusive "no diffraction" situation, which could indicate a >> million things including the possibility that your >> cryoprotectant was sub-optimal for data collection done using flash >> cryocooled/flash frozen crystals in a stream of >> gaseous nitrogen. > > But before throwing it in this category, be sure to take a wide-angle > oscillation, as reciprocal space is sparsely populated with small > unit cell crystals and you might miss spots altogether in a > 1 degree oscillation. > > I like to take a 5-sec 180* oscillation which gives plenty of > spots in a nice pattern for a salt crystal, and I suppose > records enough spacings to positively identify the mineral > if anyone cared to tak the time. > eab >>