Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 92-98 |
| Number of pages | 7 |
| Journal | Journal of Synchrotron Radiation |
| Volume | 14 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2007 |
Keywords
- Methylamine dehydrogenase
- Reaction intermediates
- Single-crystal microspectrophotometry
- Structural enzymology
- Tryptophan tryptophylquinone