Discrimination of solvent from protein regions in native Fouriers as a means of evaluating heavy-atom solutions in the MIR and MAD methods
Open Access
- 1 February 1999
- journal article
- research article
- Published by International Union of Crystallography (IUCr) in Acta Crystallographica Section D-Biological Crystallography
- Vol. 55 (2) , 501-505
- https://doi.org/10.1107/s0907444998012657
Abstract
An automated examination of the native Fourier is tested as a means of evaluation of a heavy-atom solution in MAD and MIR methods for macromolecular crystallography. It is found that the presence of distinct regions of high and low density variation in electron-density maps is a good indicator of the correctness of a heavy-atom solution in the MIR and MAD methods. The method can be used to evaluate heavy-atom solutions during MAD and MIR structure solutions and to determine the handedness of the structure if anomalous data have been measured.Keywords
This publication has 6 references indexed in Scilit:
- Using genetic algorithms for solving heavy-atom sitesActa Crystallographica Section D-Biological Crystallography, 1994
- Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondriaNature, 1994
- Structure of the gene V protein of bacteriophage f1 determined by multiwavelength x-ray diffraction on the selenomethionyl protein.Proceedings of the National Academy of Sciences, 1994
- Uniqueness and the ab initio phase problem in macromolecular crystallographyActa Crystallographica Section D-Biological Crystallography, 1993
- IMPROVING CRYSTALLOGRAPHIC MACROMOLECULAR IMAGES: THE REAL-SPACE APPROACHAnnual Review of Biophysics, 1987
- Resolution of phase ambiguity in macromolecular crystallographyPublished by Elsevier ,1985