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  ProteoPlex: Stability optimization of macromolecular complexes by sparse-matrix screening of chemical space.

Chari, A., Haselbach, D., Kirves, J. M., Ohmer, J., Paknia, E., Fischer, N., et al. (2015). ProteoPlex: Stability optimization of macromolecular complexes by sparse-matrix screening of chemical space. Nature Methods, 12(9), 859-865. doi:10.1038/NMETH.3493.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-665D-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-795C-F
Genre: Journal Article

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 Creators:
Chari, A.1, Author              
Haselbach, D.1, Author              
Kirves, J. M.1, Author              
Ohmer, J., Author
Paknia, E., Author
Fischer, N.1, Author              
Ganichkin, O.2, Author              
Moller, V., Author
Frye, J. J., Author
Petzold, G., Author
Jarvis, M., Author
Tietzel, M., Author
Grimm, C., Author
Peters, J. M., Author
Schulman, B. A., Author
Tittmann, K., Author
Markl, J., Author
Fischer, U., Author
Stark, H.1, Author              
Affiliations:
1Research Group of 3D Electron Cryo-Microscopy, MPI for Biophysical Chemistry, Max Planck Society, ou_578577              
2Research Group of X-Ray Crystallography, MPI for biophysical chemistry, Max Planck Society, ou_578578              

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 Abstract: Molecular machines or macromolecular complexes are supramolecular assemblies of biomolecules with a variety of functions. Structure determination of these complexes in a purified state is often tedious owing to their compositional complexity and the associated relative structural instability. To improve the stability of macromolecular complexes in vitro, we present a generic method that optimizes the stability, homogeneity and solubility of macromolecular complexes by sparse-matrix screening of their thermal unfolding behavior in the presence of various buffers and small molecules. The method includes the automated analysis of thermal unfolding curves based on a biophysical unfolding model for complexes. We found that under stabilizing conditions, even large multicomponent complexes reveal an almost ideal two-state unfolding behavior. We envisage an improved biochemical understanding of purified macromolecules as well as a substantial boost in successful macromolecular complex structure determination by both X-ray crystallography and cryo-electron microscopy.

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Language(s): eng - English
 Dates: 2015-08-032015-09
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/NMETH.3493
 Degree: -

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Title: Nature Methods
Source Genre: Journal
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Pages: - Volume / Issue: 12 (9) Sequence Number: - Start / End Page: 859 - 865 Identifier: -