Protein microcrystal diffraction and the effects of radiation damage with ultra-high-flux synchrotron radiation.

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Abstract
By using ultra-high-flux synchrotron x-radiation from a wiggler source, good Laue diffraction data have been obtained from protein microcrystals of size 30 .times. 35 .times. 10 .mu.m3, mounted wet in glass capillaries. At the flux level of 1013-1014 photons per sec/mm2, the radiation damage is still low enough to allow a large survey of reciprocal space for a microcrystal and a complete survey for a normal-sized protein crystal. The development of sources for ultra-high-intensity synchrotron radiation is thus an important improvement in the technique for determination of structure through protein crystallography as well as in other cases where crystal size is often a limiting factor.