Robust total X-ray scattering workflow to study correlated motion of proteins in crystals.

ABSTRACT: The breathing motions of proteins are thought to play a critical role in function. However, current techniques to study key collective motions are limited to spectroscopy and computation. We present a high-resolution experimental approach based on the total scattering from protein crystals at room temperature (TS/RT-MX) that captures both structure and collective motions. To reveal the scattering signal from protein motions, we present a general workflow that enables robust subtraction of lattice disorder. The workflow introduces two methods: GOODVIBES, a detailed and refinable lattice disorder model based on the rigid-body vibrations of a crystalline elastic network; and DISCOBALL, an independent method of validation that estimates the displacement covariance between proteins in the latti

SUBMITTER: Meisburger SP 

PROVIDER: S-EPMC9984388 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature