title: Combining X-ray crystallography and single-crystal spectroscopy to probe enzyme mechanisms.
abstract: The combination of X-ray crystallography and rapid cryo-trapping methods has enabled the visualization of catalytic intermediates in a variety of enzyme systems. However, the resolution of the X-ray experiment is not always sufficient to precisely place the structure on the reaction pathway. In addition, many trapped intermediates are X-ray-sensitive and can decay during diffraction data collection, resulting in a final structure that may not be representative of the initial trapped species. Complementary methods, such as single-crystal spectroscopy, provide a means to precisely identify the cryo-trapped species as well as detect any X-ray-induced changes during diffraction data collection.
authors.affiliation: Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
authors.forename: Arwen R
authors.initials: AR
authors.lastname: Pearson
authors.forename: Robin L
authors.initials: RL
authors.lastname: Owen
mesh_terms: D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods*; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D013053:Spectrophotometry / Q000379:methods*
chemical_list: D004798:Enzymes