Crystallization and structure solution of p53 (residues 326–356) by molecular replacement using an NMR model as template
pmid: 9761820
Crystallization and structure solution of p53 (residues 326–356) by molecular replacement using an NMR model as template
The molecular replacement method is a powerful technique for crystal structure solution but the use of NMR structures as templates often causes problems. In this work the NMR structure of the p53 tetramerization domain has been used to solve the crystal structure by molecular replacement. Since the rotation- and translation-functions were not sufficiently clear, additional information about the symmetry of the crystal and the protein complex was used to identify correct solutions. The three-dimensional structure of residues 326–356 was subsequently refined to a final R factor of 19.1% at 1.5 Å resolution.
- Novartis (Switzerland) Switzerland
Models, Molecular, Solutions, Magnetic Resonance Spectroscopy, Molecular Structure, Templates, Genetic, Tumor Suppressor Protein p53, Crystallization, Protein Structure, Tertiary
Models, Molecular, Solutions, Magnetic Resonance Spectroscopy, Molecular Structure, Templates, Genetic, Tumor Suppressor Protein p53, Crystallization, Protein Structure, Tertiary
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