radiation damage
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.
Keywords: single-crystal microspectrophotometry; reaction intermediates; structural enzymology; tryptophan tryptophylquinone; methylamine dehydrogenase.
Supporting information
Graphic Interchange Format (GIF) image https://doi.org/10.1107/S0909049506051259/ms5001sup1.gif |