Abstract
A fundamental problem for structural biology in combining solution x-ray scattering data with atomic resolution structures determined by crystallography is to find effective ways to model motions accessible to molecules outside the crystal environment. Motions can be derived when multiple conformations are experimentally observed or can be inferred through computational methods such as normal modes, molecular dynamics, and Monte Carlo-based techniques. Small-angle x-ray scattering (SAXS) is a complete, resolution-limited structural measurement of the solution state for macromolecules.
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