Microspectrophotometry for structural enzymology.
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.
Pearson
Arwen R
AR
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Mozzarelli
Andrea
A
Rossi
Gian Luigi
GL
D000818:Animals; D003460:Crystallization / Q000379:methods; D003461:Crystallography / Q000295:instrumentation* / Q000379:methods* / Q000639:trends; D004789:Enzyme Activation; D004798:Enzymes / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D009862:Online Systems; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D013053:Spectrophotometry / Q000295:instrumentation* / Q000379:methods* / Q000639:trends; D013329:Structure-Activity Relationship; D013673:Technology Assessment, Biomedical
D004798:Enzymes