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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / radiation effects*
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Bacterial Proteins / ultrastructure
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Dose-Response Relationship, Radiation
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Multiprotein Complexes / chemistry
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Multiprotein Complexes / radiation effects
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Multiprotein Complexes / ultrastructure
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Oxidation-Reduction / radiation effects
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Oxidoreductases Acting on CH-NH Group Donors / chemistry*
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Oxidoreductases Acting on CH-NH Group Donors / radiation effects*
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Oxidoreductases Acting on CH-NH Group Donors / ultrastructure
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Paracoccus denitrificans / enzymology*
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Protein Conformation / radiation effects
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Radiation Dosage
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Spectrophotometry, Ultraviolet / methods*
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X-Rays
Substances
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Bacterial Proteins
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Multiprotein Complexes
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mauC protein, Methylobacterium extorquens
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methylamine dehydrogenase
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Oxidoreductases Acting on CH-NH Group Donors