Abstract
Direct methods have successfully been used to break the phase ambiguity intrinsic in the single isomorphous replacement (SIR) data of proteins. Based on this, the procedure 'direct-method-aided MIR phasing' (DMIR) has been proposed and applied to the four-derivative multiple isomorphous replacement (MIR) data of a known protein containing 682 amino acid residuals in the asymmetric unit. The data set consists of 14,500 unique reflections at 3 A resolution with F(obs.) greater than 2sigma. Test calculation showed that the phases from conventional MIR phasing could be significantly improved by direct methods leading to obvious improvement in the quality of the resultant Fourier maps.
Published Version
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Schedule a callMore From: Acta crystallographica. Section A, Foundations of crystallography
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