2j56
X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE N-SEMIQUINONE IN COMPLEX WITH AMICYANIN.
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, resolution 2.10Å | |||||||
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Sites: | |||||||
Ligands: | , and | ||||||
Activity: | Amine dehydrogenase, with EC number 1.4.99.3 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
OverviewOverview
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.
About this StructureAbout this Structure
2J56 is a Protein complex structure of sequences from Paracoccus denitrificans. Full crystallographic information is available from OCA.
ReferenceReference
Tracking X-ray-derived redox changes in crystals of a methylamine dehydrogenase/amicyanin complex using single-crystal UV/Vis microspectrophotometry., Pearson AR, Pahl R, Kovaleva EG, Davidson VL, Wilmot CM, J Synchrotron Radiat. 2007 Jan;14(Pt 1):92-8. Epub 2006 Dec 15. PMID:17211075
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