Crystallization of RNA polymerase I subcomplex A14/A43 by iterative prediction, probing and removal of flexible regions

Title data

Geiger, Sebastian R. ; Kuhn, Claus-D. ; Leidig, Christoph ; Renkawitz, Jörg ; Cramer, Patrick:
Crystallization of RNA polymerase I subcomplex A14/A43 by iterative prediction, probing and removal of flexible regions.
In: Acta Crystallographica Section F. Vol. 64 (2008) Issue 5 . - pp. 413-418.
ISSN 2053-230X
DOI: https://doi.org/10.1107/S174430910800972X

Official URL:

Abstract in another language

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.

Further data

Item Type:	Article in a journal
Refereed:	Yes
Keywords:	Amino Acid Sequence; Cloning, Molecular; Computational Biology; Crystallization/*methods; Crystallography, X-Ray; Dimerization; Models, Molecular; Molecular Sequence Data; *Protein Engineering; Protein Structure, Tertiary; RNA Polymerase I/*chemistry/metabolism/physiology; RNA Polymerase II/metabolism; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins/chemistry/metabolism; Sequence Homology, Amino Acid
Institutions of the University:	Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry Profile Fields > Advanced Fields > Molecular Biosciences Research Institutions > Research Centres > Bayreuth Center for Molecular Biosciences - BZMB Faculties Faculties > Faculty of Biology, Chemistry and Earth Sciences Profile Fields Profile Fields > Advanced Fields Research Institutions Research Institutions > Research Centres
Result of work at the UBT:	No
DDC Subjects:	500 Science > 570 Life sciences, biology
Date Deposited:	10 Jan 2017 11:14
Last Modified:	10 Jan 2017 11:14
URI:	https://eref.uni-bayreuth.de/id/eprint/35641