Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data.

Publication Type:

Journal Article


Acta Crystallogr D Biol Crystallogr, Volume 60, Issue Pt 9, p.1579-85 (2004)


Algorithms, Data Interpretation, Statistical, Fourier Analysis, Insulin, Linear Models, Protein Conformation, Proteins, X-Ray Diffraction


<p>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.</p>