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1aie
From Proteopedia
| 1aie, resolution 1.50Å () | |||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE
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 A resolution.
Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template., Mittl PR, Chene P, Grutter MG, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):86-9. PMID:9761820
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1aie is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Mittl PR, Chene P, Grutter MG. Crystallization and structure solution of p53 (residues 326-356) by molecular replacement using an NMR model as template. Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):86-9. PMID:9761820
- Bhattacharyya R, Samanta U, Chakrabarti P. Aromatic-aromatic interactions in and around alpha-helices. Protein Eng. 2002 Feb;15(2):91-100. PMID:11917145
- Alibes A, Yankilevich P, Canada A, Diaz-Uriarte R. IDconverter and IDClight: conversion and annotation of gene and protein IDs. BMC Bioinformatics. 2007 Jan 10;8:9. PMID:17214880 doi:10.1186/1471-2105-8-9

