Abstract
Diffuse scattering analyses are emerging as a technique to extract additional dynamic information from x-ray diffraction data. In fact, when examined carefully, most protein crystals show significant diffuse scattering in addition to the usual Bragg diffraction. This diffuse scattering contains information about the disorder in the crystal that cannot be obtained from the Bragg diffraction data. Diffraction from tropomyosin crystals shows characteristic diffuse scattering streaks that are directly related to motion of the molecules. The structure of tropomyosin to 15 A resolution shows that the limited molecular contacts between molecules allow large conformational fluctuations of up to 8 A amplitude. Models for the three-dimensional motion of tropomyosin have been tested by comparing their predicted diffuse scattering patterns with the experimental data. From the parameters of the successful simulations, we were able to determine the amplitudes, directions, and distances over which the atomic displacements are correlated.