Arwen R Pearson, Reinhard Pahl, Elena G Kovaleva, Victor L Davidson, Carrie M Wilmot
Department of Biochemistry, Molecular Biology and Biophysics, The University of Minnesota, Minneapolis, MN 55455, USA.
Journal of synchrotron radiation 2007 JanX-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.
Arwen R Pearson, Reinhard Pahl, Elena G Kovaleva, Victor L Davidson, Carrie M Wilmot. Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry. Journal of synchrotron radiation. 2007 Jan;14(Pt 1):92-8
PMID: 17211075
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