Crystallization of RNA polymerase I subcomplex A14/A43 by iterative prediction, probing and removal of flexible regions
| Autor: | Jörg Renkawitz, Christoph Leidig, Claus-D. Kuhn, Sebastian R. Geiger, Patrick Cramer |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Molecular Sequence Data Saccharomyces cerevisiae Biophysics RNA polymerase II macromolecular substances Computational biology Crystallography X-Ray Protein Engineering Biochemistry law.invention RNA Polymerase I Structural Biology law Genetics RNA polymerase I Amino Acid Sequence Cloning Molecular Crystallization Peptide sequence Sequence Homology Amino Acid biology Computational Biology A protein Protein engineering Condensed Matter Physics biology.organism_classification Protein Structure Tertiary Crystallization Communications biology.protein RNA Polymerase II Dimerization Macromolecule |
| Zdroj: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s174430910800972x |
| Popis: | The removal of flexible protein regions is generally used to promote crystallization, but advanced strategies to quickly remove multiple flexible regions from proteins or protein complexes are lacking. Here, it is shown how a protein heterodimer with multiple flexibilities, the RNA polymerase I subcomplex A14/A43, could be crystallized with the use of an iterative procedure of predicting flexible regions, experimentally testing and improving these predictions and combining deletions of flexible regions in a stepwise manner. This strategy should enable the crystallization of other proteins and subcomplexes with multiple flexibilities, as required for hybrid structure solution of large macromolecular assemblies. |
| Databáze: | OpenAIRE |
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