Time-resolved Laue Crystallography as a Technique to Study the Structural Dynamics of Proteins

Abstract

We have collected a series of single-exposure Laue diffraction data from trigonal crystals of bovine pancreatic ribonuclease A at the Beam Line 18B in the Photon Factory synchrotron radiation source. Omit Fourier difference maps clearly showed the sulfate anion molecule or the 3'-uridylic acid molecule bound to the catalytic center of ribonuclease A. For time-resolved X-ray crystallographic analyses of biological macromolecules, it is critical to efficiently collect sufficient data for analyzing the target molecule during a single Laue exposure. To accomplish this, it is essential to use a high symmetry crystal and a large size detector.