Abstract
An improved method of crystallographic structure refinement, especially suitable for large molecules, is described, it is based on simultaneous minimization of a realistic potential-energy function and a crystallographic residual. The method has already proved its worth in the final stages of refinement of two structures; an application to crude wiremodel coordinates of a small protein is described and evaluated.
Publisher
International Union of Crystallography (IUCr)
Cited by
426 articles.
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