Evidence map›Paper›PMID 18453714›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008

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

Sebastian R Geiger, Claus D Kuhn, Christoph Leidig, Jörg Renkawitz, Patrick Cramer

Abstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Sebastian R GeigerGene Center Munich, Center for Integrated Protein Science (CIPSM) and Department of Chemistry and Biochemistry, Ludwig-Maximilians-Universität München, Feodor-Lynen-Strasse 25, 81377 Munich, Germany.
Claus D Kuhn
Christoph Leidig
Jörg Renkawitz
Patrick Cramer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Protein EngineeringAmino Acid SequenceCloning, MolecularComputational BiologyCrystallizationCrystallography, X-RayDimerizationModels, MolecularMolecular Sequence DataProtein Structure, TertiaryRNA Polymerase IRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidRNA Polymerase IRNA Polymerase IIRPB7 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID18453714
PMCPMC2376391

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.