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A microspectrophotometer for cryogenic protein crystallography is described. It is capable of measuring visible absorption spectra (350–800 nm) of a single crystal during X-ray data collection. The microspectrophotometer is designed to minimize the level of stray light by using a double monochromator and an optical microscope equipped with two field diaphragms and a pinhole. In this system, a thick crystal with an optical density of ∼5 is measurable. In order to demonstrate the performance of the system, the absorption spectra of the unphotolyzed state and the primary photoreaction intermediate of bacteriorhodopsin in the P622 crystal have been measured under a flow of cold nitrogen gas at 100 K.

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