Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data.
A new experimental strategy is described for obtaining time-resolved protein structural changes using monochromatic X-ray crystallographic data. The method is based on time-dependent linear interpolation of observed intensity variations during conventional X-ray diffraction data collection. The method benefits from high data redundancy. Although the method was developed to examine time-dependent X-ray-induced crystal decay, it is potentially applicable to a variety of time-dependent crystallographic studies, including structural determination of chemical intermediates in enzyme reactions and X-ray-induced unfolding of proteins with multiple disulfide bonds.
Wang
Jun
J
Department of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853, USA.
Ealick
Steven E
SE
D000465:Algorithms; D003627:Data Interpretation, Statistical; D005583:Fourier Analysis; D007328:Insulin / Q000737:chemistry; D016014:Linear Models; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000706:statistics & numerical data*
D007328:Insulin; D011506:Proteins