Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography.
Advances in the adaptation of optical spectroscopy to monitor photo-induced or enzyme-catalyzed reactions in the crystalline state have enabled X-ray crystal structures to be accurately linked with spectroscopically defined intermediates. This, in turn, has led to a deeper understanding of the role protein structural changes play in function. The integration of optical spectroscopy with X-ray crystallography is growing and now extends beyond linking crystal structure to reaction intermediate. Recent examples of this synergy include applications in protein crystallization, X-ray data acquisition, radiation damage, and acquisition of phase information important for structure determination.
De la Mora-Rey
Teresa
T
Department of Biochemistry, Molecular Biology & Biophysics, University of Minnesota, Minneapolis 55455, USA.
Wilmot
Carrie M
CM
D003460:Crystallization; D018360:Crystallography, X-Ray / Q000295:instrumentation / Q000379:methods*; D007700:Kinetics; D008958:Models, Molecular; D015394:Molecular Structure; D009097:Multienzyme Complexes / Q000737:chemistry; D046912:Multiprotein Complexes / Q000737:chemistry; D020283:Photoreceptors, Microbial / Q000737:chemistry; D013053:Spectrophotometry / Q000295:instrumentation / Q000379:methods*
D009097:Multienzyme Complexes; D046912:Multiprotein Complexes; D020283:Photoreceptors, Microbial