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Updated: Sep 27, 2026

Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies
Published on: April 11, 2021
How does radiation damage in protein crystals depend on X-ray dose?
Piotr Sliz1, Stephen C Harrison, Gerd Rosenbaum
1Department of Biological Chemistry and Molecular Pharmacology, Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115, USA.
Abstract:
Is radiation damage to cryopreserved protein crystals strictly proportional to accumulated dose at the high-flux density of beams from undulators at third-generation synchrotron sources? The answer is "yes," for overall damage to several different kinds of protein crystals at flux densities up to 10(15) ph/sec/mm(2) (APS beamline 19-ID). We find that, at 12 keV (1 A wavelength), about ten absorbed photons are sufficient to "kill" a unit cell. As this corresponds to about one elastically scattered photon, each unit cell can contribute only about one photon to total Bragg diffraction. The smallest crystal that can yield a full data set to 3.5 A resolution has a diameter of about 20 microm (100 A unit cell).
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