Abstract
A general class of iterative projection algorithms is described and proposed as a tool for phasing in protein crystallography in order to improve the radius of convergence over that of conventional density-modification algorithms. Their relationship to conventional density modification is described. The common iterative projection algorithms, their convergence properties and their application to protein crystallography are described. These algorithms offer the possibility of protein structure determination starting with only information on the molecular envelope and low-order non-crystallographic symmetry.
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