View full size JPG | PDF George Retseck
Making high-quality crystals large enough to usefully diffract X-rays is a major headache when attempting to determine protein structures by X-ray crystallography. Researchers prefer crystals that are 100–200 microns in size, with 5 microns being the smallest crystals that can be examined using a synchrotron X-ray source. More powerful X-rays provide better diffraction, but damage the crystals.








