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Wiley InterScience

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Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry
Arwen R. Pearson Reinhard Pahl Elena G. Kovaleva Victor L. Davidson Carrie M. Wilmot
Copyright International Union of Crystallography, 2007
KEYWORDS
single-crystal microspectrophotometry • reaction intermediates • structural enzymology • tryptophan tryptophylquinone • methylamine dehydrogenase.

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.


Received 26 May 2006, accepted 27 November 2006

DIGITAL OBJECT IDENTIFIER (DOI)
10.1107/S0909049506051259 About DOI

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