Exploiting tertiary structure through local folds for crystallographic phasing

We describe an algorithm for phasing protein crystal X-ray diffraction data that identifies, retrieves, refines and exploits general tertiary structural information from small fragments available in the Protein Data Bank. The algorithm successfully phased, through unspecific molecular replacement combined with density modification, all-helical, mixed alpha-beta, and all-beta protein structures. The method is available as a software implementation: Borges.This work was supported by the Spanish Ministerio de Ciencia e Innovación-Ministerio de Economia y Competitividad, Centro de Desarrollo Tecnológico Industrial and Consejo Superior de Investigaciones Científicas (grants BIO2009-10576; IDC-2010-1173; BFU2012-35367; BFU2012-32847; predoctoral grants to D.D.R., I.D.M. and I.M.d.I.; JdC to K.M.; RyC to R.M.B.); Generalitat de Catalunya (2009SGR-1036); VW-Stiftung Niedersachsenprofessur to G.M.S.Peer reviewe