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PubMed · 15582388

Microspectrophotometry for structural enzymology.

Arwen R Pearson·Andrea Mozzarelli·Gian Luigi Rossi
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Abstract

For several decades, single-crystal microspectrophotometry has contributed to structural enzymology as a very useful complement to X-ray crystallography. In its most recent applications, it is the ideal tool to track chemistry as structure evolves in the course of time-resolved experiments, to identify freeze-trapped catalytic intermediates and to assess radiation-induced effects on enzyme crystals. To these goals, instruments have been developed to record optical spectra 'on-line' in the course of X-ray data collection, whereas more rigorous polarized absorption studies 'off-line' play an essential role in describing what protein function is retained in the crystalline state and correlating it with the observed structures.

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AnimalsCrystallizationCrystallographyEnzyme ActivationEnzymesHumansOnline SystemsProtein ConformationProtein Structure, TertiarySpectrophotometryStructure-Activity RelationshipTechnology Assessment, BiomedicalJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, P.H.S.Review

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Arwen R Pearson, Andrea Mozzarelli, Gian Luigi Rossi. 2004. Microspectrophotometry for structural enzymology.. https://doi.org/10.1016/j.sbi.2004.10.007

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