X-ray crystallography and NMR spectroscopy are two powerful tools to determine the three-dimensional structures and characterize the dynamic properties of proteins. The two methods are now combined to structurally unravel interconverting substrates of a human proline isomerase. Crystallographic approaches are used to define minor protein conformations and, combined with NMR analysis, to show how collective motions contribute to the catalytic power of an enzyme.
- James S. Fraser
- Michael W. Clarkson
- Tom Alber
