Combining X-ray crystallography and single-crystal spectroscopy to probe enzyme mechanisms.
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.
Pearson
Arwen R
AR
Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
Owen
Robin L
RL
D002384:Catalysis; D018360:Crystallography, X-Ray / Q000379:methods*; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D013053:Spectrophotometry / Q000379:methods*
D004798:Enzymes