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X-ray exposure during crystallographic data collection can result in unintended redox changes in proteins containing functionally important redox centers. In order to directly monitor X-ray-derived redox changes in trapped oxidative half-reaction intermediates of Paracoccus denitrificans methylamine dehydrogenase, a commercially available single-crystal UV/Vis microspectrophotometer was installed on-line at the BioCARS beamline 14-BM-C at the Advanced Photon Source, Argonne, USA. Monitoring the redox state of the intermediates during X-ray exposure permitted the creation of a general multi-crystal data collection strategy to generate true structures of each redox intermediate.

Supporting information


Graphic Interchange Format (GIF) image
Movie showing a series of single-crystal spectra recorded as a TTQ_OX / Cu^2+ MADH/amicyanin crystal is rotated about angle phi. The anisotropic nature of single-crystal spectra is clearly observed.

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