2j55: Difference between revisions

Revision as of 09:46, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2j55.png

Template:STRUCTURE 2j55

X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.

Template:ABSTRACT PUBMED 17211075

About this StructureAbout this Structure

2J55 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

Page seeded by OCA on Tue Jul 29 09:46:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.'''
+===X-RAY REDUCED PARACCOCUS DENITRIFICANS METHYLAMINE DEHYDROGENASE O-QUINONE IN COMPLEX WITH AMICYANIN.===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17211075}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_17211075}}
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